| FFPE DNA extraction protocol using the Bioruptor® The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, provid... | Download |
Proteinase K is a non-specific serine protease. This ChIP grade product has been extensively validated to isolate the DNA from the Immunoprecipitated (IP’d) chromatin. It is included in our OneDay ChIP KIT (cat# kch-onedIP-060, -180) and our LowCell# ChIP KIT (cat# kch-maglow-016). It is now separately available.
| FFPE DNA extraction protocol using the Bioruptor® The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, provid... | Download |
| Datasheet ProteinaseK kch-507-100 DATASHEET Datasheet description | Download |
 How to properly cite this product in your workDiagenode strongly recommends using this: Proteinase K, 100 µl (Diagenode Cat# C06050001). Click here to copy to clipboard. Using our products in your publication? Let us know! |
Aging-regulated anti-apoptotic long non-coding RNA Sarrah augments recovery from acute myocardial infarction. |
The endocannabinoid anandamide has an anti-inflammatory effect on CCL2 expression in vascular smooth muscle cells. |
The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase. |
Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function. |
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Aging is the major risk factor for cardiovascular disease with cardiomyocyte apoptosis as one underlying cause. Here, we report the identification of the aging-regulated lncRNA Sarrah (ENSMUST00000140003) that is anti-apoptotic in cardiomyocytes. Importantly, loss of SARRAH (OXCT1-AS1) in human engineered heart tissue results in impaired contractile force development. SARRAH directly binds to the promoters of genes downregulated after SARRAH silencing via RNA-DNA triple helix formation and cardiomyocytes lacking the triple helix forming domain of Sarrah show an increase in apoptosis. One of the direct SARRAH targets is NRF2, and restoration of NRF2 levels after SARRAH silencing partially rescues the reduction in cell viability. Overexpression of Sarrah in mice shows better recovery of cardiac contractile function after AMI compared to control mice. In summary, we identified the anti-apoptotic evolutionary conserved lncRNA Sarrah, which is downregulated by aging, as a regulator of cardiomyocyte survival.</p>', 'date' => '2020-04-27', 'pmid' => 'http://www.pubmed.gov/32341350', 'doi' => '10.1038/s41467-020-15995-2', 'modified' => '2020-08-17 10:30:19', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '3933', 'name' => 'The endocannabinoid anandamide has an anti-inflammatory effect on CCL2 expression in vascular smooth muscle cells.', 'authors' => 'Pflüger-Müller B, Oo JA, Heering J, Warwick T, Proschak E, Günther S, Looso M, Rezende F, Fork C, Geisslinger G, Thomas D, Gurke R, Steinhilber D, Schulz M, Leisegang MS, Brandes RP', 'description' => '<p>Endocannabinoids are important lipid-signaling mediators. Both protective and deleterious effects of endocannabinoids in the cardiovascular system have been reported but the mechanistic basis for these contradicting observations is unclear. We set out to identify anti-inflammatory mechanisms of endocannabinoids in the murine aorta and in human vascular smooth muscle cells (hVSMC). In response to combined stimulation with cytokines, IL-1β and TNFα, the murine aorta released several endocannabinoids, with anandamide (AEA) levels being the most significantly increased. AEA pretreatment had profound effects on cytokine-induced gene expression in hVSMC and murine aorta. As revealed by RNA-Seq analysis, the induction of a subset of 21 inflammatory target genes, including the important cytokine CCL2 was blocked by AEA. This effect was not mediated through AEA-dependent interference of the AP-1 or NF-κB pathways but rather through an epigenetic mechanism. In the presence of AEA, ATAC-Seq analysis and chromatin-immunoprecipitations revealed that CCL2 induction was blocked due to increased levels of H3K27me3 and a decrease of H3K27ac leading to compacted chromatin structure in the CCL2 promoter. These effects were mediated by recruitment of HDAC4 and the nuclear corepressor NCoR1 to the CCL2 promoter. This study therefore establishes a novel anti-inflammatory mechanism for the endogenous endocannabinoid AEA in vascular smooth muscle cells. Furthermore, this work provides a link between endogenous endocannabinoid signaling and epigenetic regulation.</p>', 'date' => '2020-04-22', 'pmid' => 'http://www.pubmed.gov/32323032', 'doi' => '10.1007/s00395-020-0793-3', 'modified' => '2020-08-17 10:39:12', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '3407', 'name' => 'The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase.', 'authors' => 'Vasconez AE, Janetzko P, Oo JA, Pflüger-Müller B, Ratiu C, Gu L, Helin K, Geisslinger G, Fleming I, Schröder K, Fork C, Brandes RP, Leisegang MS', 'description' => '<p>AIM: The histone demethylase Jarid1b limits gene expression by removing the active methyl mark from histone3 lysine4 at gene promoter regions. A vascular function of Jarid1b is unknown, but a vasoprotective function to inflammatory and hypertrophic stimuli, like angiotensin II (AngII) could be inferred. This hypothesis was tested using Jarid1b knockout mice and the inhibitor PBIT. METHODS: Mice or aortic segments were treated with AngII to induce endothelial dysfunction. Aortae from WT and Jarid1b knockout were studied in organ chambers and endothelium-dependent dilator responses to acetylcholine and endothelium-independent responses to DetaNONOate were recorded after pre-constriction with phenylephrine in the presence or absence of the NO-synthase inhibitor nitro-L-arginine. Molecular mechanisms were investigated with chromatin immunoprecipitation, RNA-Seq, RNA-3'-adaptor-ligation, actinomycin D and RNA-immunoprecipitation. RESULTS: Knockout or inhibition of Jarid1b prevented the development of endothelial dysfunction in response to AngII. This effect was not a consequence of altered nitrite oxide availability but accompanied by a loss of the inflammatory response to AngII. As Jarid1b mainly inhibits gene expression, an indirect effect should account for this observation. AngII induced the soluble epoxide hydrolase (sEH), which degrades anti-inflammatory lipids, and thus promotes inflammation. Knockout or inhibition of Jarid1b prevented the AngII-mediated sEH induction. Mechanistically, Jarid1b maintained the length of the 3'untranslated region of the sEH mRNA, thereby increasing its stability and thus sEH protein expression. Loss of Jarid1b activity therefore resulted in sEH mRNA destabilization. CONCLUSION: Jarid1b contributes to the pro-inflammatory effects of AngII by stabilizing sEH expression. Jarid1b inhibition might be an option for future therapeutics against cardiovascular dysfunction.</p>', 'date' => '2018-08-04', 'pmid' => 'http://www.pubmed.gov/30076673', 'doi' => '10.1111/apha.13168', 'modified' => '2018-11-09 11:18:29', 'created' => '2018-11-08 12:59:45', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array( (int) 0 => array( 'id' => '864', 'name' => 'Proteinase K SDS US en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-US-en-GHS_1_0.pdf', 'countries' => 'US', 'modified' => '2020-09-22 14:21:25', 'created' => '2020-09-22 14:21:25', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '862', 'name' => 'Proteinase K SDS GB en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-GB-en-GHS_1_0.pdf', 'countries' => 'GB', 'modified' => '2020-09-22 14:20:24', 'created' => '2020-09-22 14:20:24', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '857', 'name' => 'Proteinase K SDS BE fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-fr-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:02', 'created' => '2020-09-22 14:18:02', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '861', 'name' => 'Proteinase K SDS FR fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-FR-fr-GHS_1_0.pdf', 'countries' => 'FR', 'modified' => '2020-09-22 14:19:56', 'created' => '2020-09-22 14:19:56', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 4 => array( 'id' => '860', 'name' => 'Proteinase K SDS ES es', 'language' => 'es', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-ES-es-GHS_1_0.pdf', 'countries' => 'ES', 'modified' => '2020-09-22 14:19:27', 'created' => '2020-09-22 14:19:27', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 5 => array( 'id' => '859', 'name' => 'Proteinase K SDS DE de', 'language' => 'de', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-DE-de-GHS_1_0.pdf', 'countries' => 'DE', 'modified' => '2020-09-22 14:18:55', 'created' => '2020-09-22 14:18:55', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 6 => array( 'id' => '863', 'name' => 'Proteinase K SDS JP ja', 'language' => 'ja', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-JP-ja-GHS_1_0.pdf', 'countries' => 'JP', 'modified' => '2020-09-22 14:20:54', 'created' => '2020-09-22 14:20:54', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 7 => array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( [maximum depth reached] ) ) ) ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(kch-507-100)</span></small>' $country_code = 'US' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $protocol = array( 'id' => '10', 'name' => 'FFPE DNA extraction protocol using the Bioruptor®', 'description' => '<p><span>The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, providing an invaluable repository of information for genetic analysis. 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The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( 'id' => '3292', 'product_id' => '1934', 'publication_id' => '3541' ) ) $externalLink = ' <a href="http://www.pubmed.gov/29408197" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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These samples can be analyzed for a wealth of applications including biomarker discovery, drug development, and cancer research. </span><span>Diagenode’s FFPE DNA Extraction kit is optimized for the extraction of DNA from FFPE tissue sections in conjunction with the Bioruptor</span><span>®</span><span>. </span></p>', 'image_id' => '204', 'type' => 'Protocol', 'url' => 'files/protocols/FFPE_DNA_extraction_protocol.pdf', 'slug' => 'ffpe-dna-extraction-protocol', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2016-04-29 17:42:46', 'created' => '2015-07-20 10:35:07', 'ProductsProtocol' => array( [maximum depth reached] ) ) ), 'Publication' => array( (int) 0 => array( 'id' => '3938', 'name' => 'Aging-regulated anti-apoptotic long non-coding RNA Sarrah augments recovery from acute myocardial infarction.', 'authors' => 'Trembinski DJ, Bink DI, Theodorou K, Sommer J, Fischer A, van Bergen A, Kuo CC, Costa IG, Schürmann C, Leisegang MS, Brandes RP, Alekseeva T, Brill B, Wietelmann A, Johnson CN, Spring-Connell A, Kaulich M, Werfel S, Engelhardt S, Hirt MN, Yorgan K, Eschen', 'description' => '<p>Long non-coding RNAs (lncRNAs) contribute to cardiac (patho)physiology. Aging is the major risk factor for cardiovascular disease with cardiomyocyte apoptosis as one underlying cause. Here, we report the identification of the aging-regulated lncRNA Sarrah (ENSMUST00000140003) that is anti-apoptotic in cardiomyocytes. Importantly, loss of SARRAH (OXCT1-AS1) in human engineered heart tissue results in impaired contractile force development. SARRAH directly binds to the promoters of genes downregulated after SARRAH silencing via RNA-DNA triple helix formation and cardiomyocytes lacking the triple helix forming domain of Sarrah show an increase in apoptosis. One of the direct SARRAH targets is NRF2, and restoration of NRF2 levels after SARRAH silencing partially rescues the reduction in cell viability. Overexpression of Sarrah in mice shows better recovery of cardiac contractile function after AMI compared to control mice. In summary, we identified the anti-apoptotic evolutionary conserved lncRNA Sarrah, which is downregulated by aging, as a regulator of cardiomyocyte survival.</p>', 'date' => '2020-04-27', 'pmid' => 'http://www.pubmed.gov/32341350', 'doi' => '10.1038/s41467-020-15995-2', 'modified' => '2020-08-17 10:30:19', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '3933', 'name' => 'The endocannabinoid anandamide has an anti-inflammatory effect on CCL2 expression in vascular smooth muscle cells.', 'authors' => 'Pflüger-Müller B, Oo JA, Heering J, Warwick T, Proschak E, Günther S, Looso M, Rezende F, Fork C, Geisslinger G, Thomas D, Gurke R, Steinhilber D, Schulz M, Leisegang MS, Brandes RP', 'description' => '<p>Endocannabinoids are important lipid-signaling mediators. Both protective and deleterious effects of endocannabinoids in the cardiovascular system have been reported but the mechanistic basis for these contradicting observations is unclear. We set out to identify anti-inflammatory mechanisms of endocannabinoids in the murine aorta and in human vascular smooth muscle cells (hVSMC). In response to combined stimulation with cytokines, IL-1β and TNFα, the murine aorta released several endocannabinoids, with anandamide (AEA) levels being the most significantly increased. AEA pretreatment had profound effects on cytokine-induced gene expression in hVSMC and murine aorta. As revealed by RNA-Seq analysis, the induction of a subset of 21 inflammatory target genes, including the important cytokine CCL2 was blocked by AEA. This effect was not mediated through AEA-dependent interference of the AP-1 or NF-κB pathways but rather through an epigenetic mechanism. In the presence of AEA, ATAC-Seq analysis and chromatin-immunoprecipitations revealed that CCL2 induction was blocked due to increased levels of H3K27me3 and a decrease of H3K27ac leading to compacted chromatin structure in the CCL2 promoter. These effects were mediated by recruitment of HDAC4 and the nuclear corepressor NCoR1 to the CCL2 promoter. This study therefore establishes a novel anti-inflammatory mechanism for the endogenous endocannabinoid AEA in vascular smooth muscle cells. Furthermore, this work provides a link between endogenous endocannabinoid signaling and epigenetic regulation.</p>', 'date' => '2020-04-22', 'pmid' => 'http://www.pubmed.gov/32323032', 'doi' => '10.1007/s00395-020-0793-3', 'modified' => '2020-08-17 10:39:12', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '3407', 'name' => 'The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase.', 'authors' => 'Vasconez AE, Janetzko P, Oo JA, Pflüger-Müller B, Ratiu C, Gu L, Helin K, Geisslinger G, Fleming I, Schröder K, Fork C, Brandes RP, Leisegang MS', 'description' => '<p>AIM: The histone demethylase Jarid1b limits gene expression by removing the active methyl mark from histone3 lysine4 at gene promoter regions. A vascular function of Jarid1b is unknown, but a vasoprotective function to inflammatory and hypertrophic stimuli, like angiotensin II (AngII) could be inferred. This hypothesis was tested using Jarid1b knockout mice and the inhibitor PBIT. METHODS: Mice or aortic segments were treated with AngII to induce endothelial dysfunction. Aortae from WT and Jarid1b knockout were studied in organ chambers and endothelium-dependent dilator responses to acetylcholine and endothelium-independent responses to DetaNONOate were recorded after pre-constriction with phenylephrine in the presence or absence of the NO-synthase inhibitor nitro-L-arginine. Molecular mechanisms were investigated with chromatin immunoprecipitation, RNA-Seq, RNA-3'-adaptor-ligation, actinomycin D and RNA-immunoprecipitation. RESULTS: Knockout or inhibition of Jarid1b prevented the development of endothelial dysfunction in response to AngII. This effect was not a consequence of altered nitrite oxide availability but accompanied by a loss of the inflammatory response to AngII. As Jarid1b mainly inhibits gene expression, an indirect effect should account for this observation. AngII induced the soluble epoxide hydrolase (sEH), which degrades anti-inflammatory lipids, and thus promotes inflammation. Knockout or inhibition of Jarid1b prevented the AngII-mediated sEH induction. Mechanistically, Jarid1b maintained the length of the 3'untranslated region of the sEH mRNA, thereby increasing its stability and thus sEH protein expression. Loss of Jarid1b activity therefore resulted in sEH mRNA destabilization. CONCLUSION: Jarid1b contributes to the pro-inflammatory effects of AngII by stabilizing sEH expression. Jarid1b inhibition might be an option for future therapeutics against cardiovascular dysfunction.</p>', 'date' => '2018-08-04', 'pmid' => 'http://www.pubmed.gov/30076673', 'doi' => '10.1111/apha.13168', 'modified' => '2018-11-09 11:18:29', 'created' => '2018-11-08 12:59:45', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array( (int) 0 => array( 'id' => '864', 'name' => 'Proteinase K SDS US en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-US-en-GHS_1_0.pdf', 'countries' => 'US', 'modified' => '2020-09-22 14:21:25', 'created' => '2020-09-22 14:21:25', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '862', 'name' => 'Proteinase K SDS GB en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-GB-en-GHS_1_0.pdf', 'countries' => 'GB', 'modified' => '2020-09-22 14:20:24', 'created' => '2020-09-22 14:20:24', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '857', 'name' => 'Proteinase K SDS BE fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-fr-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:02', 'created' => '2020-09-22 14:18:02', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '861', 'name' => 'Proteinase K SDS FR fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-FR-fr-GHS_1_0.pdf', 'countries' => 'FR', 'modified' => '2020-09-22 14:19:56', 'created' => '2020-09-22 14:19:56', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 4 => array( 'id' => '860', 'name' => 'Proteinase K SDS ES es', 'language' => 'es', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-ES-es-GHS_1_0.pdf', 'countries' => 'ES', 'modified' => '2020-09-22 14:19:27', 'created' => '2020-09-22 14:19:27', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 5 => array( 'id' => '859', 'name' => 'Proteinase K SDS DE de', 'language' => 'de', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-DE-de-GHS_1_0.pdf', 'countries' => 'DE', 'modified' => '2020-09-22 14:18:55', 'created' => '2020-09-22 14:18:55', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 6 => array( 'id' => '863', 'name' => 'Proteinase K SDS JP ja', 'language' => 'ja', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-JP-ja-GHS_1_0.pdf', 'countries' => 'JP', 'modified' => '2020-09-22 14:20:54', 'created' => '2020-09-22 14:20:54', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 7 => array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( [maximum depth reached] ) ) ) ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(kch-507-100)</span></small>' $country_code = 'US' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $protocol = array( 'id' => '10', 'name' => 'FFPE DNA extraction protocol using the Bioruptor®', 'description' => '<p><span>The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, providing an invaluable repository of information for genetic analysis. These samples can be analyzed for a wealth of applications including biomarker discovery, drug development, and cancer research. </span><span>Diagenode’s FFPE DNA Extraction kit is optimized for the extraction of DNA from FFPE tissue sections in conjunction with the Bioruptor</span><span>®</span><span>. </span></p>', 'image_id' => '204', 'type' => 'Protocol', 'url' => 'files/protocols/FFPE_DNA_extraction_protocol.pdf', 'slug' => 'ffpe-dna-extraction-protocol', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2016-04-29 17:42:46', 'created' => '2015-07-20 10:35:07', 'ProductsProtocol' => array( 'id' => '51', 'product_id' => '1934', 'protocol_id' => '10' ) ) $document = array( 'id' => '136', 'name' => 'Datasheet ProteinaseK kch-507-100', 'description' => 'Datasheet description', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/reagents/Datasheet_ProteinaseK_kch-507-100.pdf', 'slug' => 'datasheet-proteinasek-kch-507-100', 'meta_keywords' => null, 'meta_description' => null, 'modified' => '2015-07-07 11:47:43', 'created' => '2015-07-07 11:47:43', 'ProductsDocument' => array( 'id' => '886', 'product_id' => '1934', 'document_id' => '136' ) ) $sds = array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( 'id' => '1538', 'product_id' => '1934', 'safety_sheet_id' => '858' ) ) $publication = array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( 'id' => '3292', 'product_id' => '1934', 'publication_id' => '3541' ) ) $externalLink = ' <a href="http://www.pubmed.gov/29408197" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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These samples can be analyzed for a wealth of applications including biomarker discovery, drug development, and cancer research. </span><span>Diagenode’s FFPE DNA Extraction kit is optimized for the extraction of DNA from FFPE tissue sections in conjunction with the Bioruptor</span><span>®</span><span>. </span></p>', 'image_id' => '204', 'type' => 'Protocol', 'url' => 'files/protocols/FFPE_DNA_extraction_protocol.pdf', 'slug' => 'ffpe-dna-extraction-protocol', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2016-04-29 17:42:46', 'created' => '2015-07-20 10:35:07', 'ProductsProtocol' => array( [maximum depth reached] ) ) ), 'Publication' => array( (int) 0 => array( 'id' => '3938', 'name' => 'Aging-regulated anti-apoptotic long non-coding RNA Sarrah augments recovery from acute myocardial infarction.', 'authors' => 'Trembinski DJ, Bink DI, Theodorou K, Sommer J, Fischer A, van Bergen A, Kuo CC, Costa IG, Schürmann C, Leisegang MS, Brandes RP, Alekseeva T, Brill B, Wietelmann A, Johnson CN, Spring-Connell A, Kaulich M, Werfel S, Engelhardt S, Hirt MN, Yorgan K, Eschen', 'description' => '<p>Long non-coding RNAs (lncRNAs) contribute to cardiac (patho)physiology. Aging is the major risk factor for cardiovascular disease with cardiomyocyte apoptosis as one underlying cause. Here, we report the identification of the aging-regulated lncRNA Sarrah (ENSMUST00000140003) that is anti-apoptotic in cardiomyocytes. Importantly, loss of SARRAH (OXCT1-AS1) in human engineered heart tissue results in impaired contractile force development. SARRAH directly binds to the promoters of genes downregulated after SARRAH silencing via RNA-DNA triple helix formation and cardiomyocytes lacking the triple helix forming domain of Sarrah show an increase in apoptosis. One of the direct SARRAH targets is NRF2, and restoration of NRF2 levels after SARRAH silencing partially rescues the reduction in cell viability. Overexpression of Sarrah in mice shows better recovery of cardiac contractile function after AMI compared to control mice. In summary, we identified the anti-apoptotic evolutionary conserved lncRNA Sarrah, which is downregulated by aging, as a regulator of cardiomyocyte survival.</p>', 'date' => '2020-04-27', 'pmid' => 'http://www.pubmed.gov/32341350', 'doi' => '10.1038/s41467-020-15995-2', 'modified' => '2020-08-17 10:30:19', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '3933', 'name' => 'The endocannabinoid anandamide has an anti-inflammatory effect on CCL2 expression in vascular smooth muscle cells.', 'authors' => 'Pflüger-Müller B, Oo JA, Heering J, Warwick T, Proschak E, Günther S, Looso M, Rezende F, Fork C, Geisslinger G, Thomas D, Gurke R, Steinhilber D, Schulz M, Leisegang MS, Brandes RP', 'description' => '<p>Endocannabinoids are important lipid-signaling mediators. Both protective and deleterious effects of endocannabinoids in the cardiovascular system have been reported but the mechanistic basis for these contradicting observations is unclear. We set out to identify anti-inflammatory mechanisms of endocannabinoids in the murine aorta and in human vascular smooth muscle cells (hVSMC). In response to combined stimulation with cytokines, IL-1β and TNFα, the murine aorta released several endocannabinoids, with anandamide (AEA) levels being the most significantly increased. AEA pretreatment had profound effects on cytokine-induced gene expression in hVSMC and murine aorta. As revealed by RNA-Seq analysis, the induction of a subset of 21 inflammatory target genes, including the important cytokine CCL2 was blocked by AEA. This effect was not mediated through AEA-dependent interference of the AP-1 or NF-κB pathways but rather through an epigenetic mechanism. In the presence of AEA, ATAC-Seq analysis and chromatin-immunoprecipitations revealed that CCL2 induction was blocked due to increased levels of H3K27me3 and a decrease of H3K27ac leading to compacted chromatin structure in the CCL2 promoter. These effects were mediated by recruitment of HDAC4 and the nuclear corepressor NCoR1 to the CCL2 promoter. This study therefore establishes a novel anti-inflammatory mechanism for the endogenous endocannabinoid AEA in vascular smooth muscle cells. Furthermore, this work provides a link between endogenous endocannabinoid signaling and epigenetic regulation.</p>', 'date' => '2020-04-22', 'pmid' => 'http://www.pubmed.gov/32323032', 'doi' => '10.1007/s00395-020-0793-3', 'modified' => '2020-08-17 10:39:12', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '3407', 'name' => 'The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase.', 'authors' => 'Vasconez AE, Janetzko P, Oo JA, Pflüger-Müller B, Ratiu C, Gu L, Helin K, Geisslinger G, Fleming I, Schröder K, Fork C, Brandes RP, Leisegang MS', 'description' => '<p>AIM: The histone demethylase Jarid1b limits gene expression by removing the active methyl mark from histone3 lysine4 at gene promoter regions. A vascular function of Jarid1b is unknown, but a vasoprotective function to inflammatory and hypertrophic stimuli, like angiotensin II (AngII) could be inferred. This hypothesis was tested using Jarid1b knockout mice and the inhibitor PBIT. METHODS: Mice or aortic segments were treated with AngII to induce endothelial dysfunction. Aortae from WT and Jarid1b knockout were studied in organ chambers and endothelium-dependent dilator responses to acetylcholine and endothelium-independent responses to DetaNONOate were recorded after pre-constriction with phenylephrine in the presence or absence of the NO-synthase inhibitor nitro-L-arginine. Molecular mechanisms were investigated with chromatin immunoprecipitation, RNA-Seq, RNA-3'-adaptor-ligation, actinomycin D and RNA-immunoprecipitation. RESULTS: Knockout or inhibition of Jarid1b prevented the development of endothelial dysfunction in response to AngII. This effect was not a consequence of altered nitrite oxide availability but accompanied by a loss of the inflammatory response to AngII. As Jarid1b mainly inhibits gene expression, an indirect effect should account for this observation. AngII induced the soluble epoxide hydrolase (sEH), which degrades anti-inflammatory lipids, and thus promotes inflammation. Knockout or inhibition of Jarid1b prevented the AngII-mediated sEH induction. Mechanistically, Jarid1b maintained the length of the 3'untranslated region of the sEH mRNA, thereby increasing its stability and thus sEH protein expression. Loss of Jarid1b activity therefore resulted in sEH mRNA destabilization. CONCLUSION: Jarid1b contributes to the pro-inflammatory effects of AngII by stabilizing sEH expression. Jarid1b inhibition might be an option for future therapeutics against cardiovascular dysfunction.</p>', 'date' => '2018-08-04', 'pmid' => 'http://www.pubmed.gov/30076673', 'doi' => '10.1111/apha.13168', 'modified' => '2018-11-09 11:18:29', 'created' => '2018-11-08 12:59:45', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array( (int) 0 => array( 'id' => '864', 'name' => 'Proteinase K SDS US en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-US-en-GHS_1_0.pdf', 'countries' => 'US', 'modified' => '2020-09-22 14:21:25', 'created' => '2020-09-22 14:21:25', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '862', 'name' => 'Proteinase K SDS GB en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-GB-en-GHS_1_0.pdf', 'countries' => 'GB', 'modified' => '2020-09-22 14:20:24', 'created' => '2020-09-22 14:20:24', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '857', 'name' => 'Proteinase K SDS BE fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-fr-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:02', 'created' => '2020-09-22 14:18:02', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '861', 'name' => 'Proteinase K SDS FR fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-FR-fr-GHS_1_0.pdf', 'countries' => 'FR', 'modified' => '2020-09-22 14:19:56', 'created' => '2020-09-22 14:19:56', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 4 => array( 'id' => '860', 'name' => 'Proteinase K SDS ES es', 'language' => 'es', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-ES-es-GHS_1_0.pdf', 'countries' => 'ES', 'modified' => '2020-09-22 14:19:27', 'created' => '2020-09-22 14:19:27', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 5 => array( 'id' => '859', 'name' => 'Proteinase K SDS DE de', 'language' => 'de', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-DE-de-GHS_1_0.pdf', 'countries' => 'DE', 'modified' => '2020-09-22 14:18:55', 'created' => '2020-09-22 14:18:55', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 6 => array( 'id' => '863', 'name' => 'Proteinase K SDS JP ja', 'language' => 'ja', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-JP-ja-GHS_1_0.pdf', 'countries' => 'JP', 'modified' => '2020-09-22 14:20:54', 'created' => '2020-09-22 14:20:54', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 7 => array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( [maximum depth reached] ) ) ) ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(kch-507-100)</span></small>' $country_code = 'US' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $protocol = array( 'id' => '10', 'name' => 'FFPE DNA extraction protocol using the Bioruptor®', 'description' => '<p><span>The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, providing an invaluable repository of information for genetic analysis. 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The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( 'id' => '3292', 'product_id' => '1934', 'publication_id' => '3541' ) ) $externalLink = ' <a href="http://www.pubmed.gov/29408197" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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These samples can be analyzed for a wealth of applications including biomarker discovery, drug development, and cancer research. </span><span>Diagenode’s FFPE DNA Extraction kit is optimized for the extraction of DNA from FFPE tissue sections in conjunction with the Bioruptor</span><span>®</span><span>. </span></p>', 'image_id' => '204', 'type' => 'Protocol', 'url' => 'files/protocols/FFPE_DNA_extraction_protocol.pdf', 'slug' => 'ffpe-dna-extraction-protocol', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2016-04-29 17:42:46', 'created' => '2015-07-20 10:35:07', 'ProductsProtocol' => array( [maximum depth reached] ) ) ), 'Publication' => array( (int) 0 => array( 'id' => '3938', 'name' => 'Aging-regulated anti-apoptotic long non-coding RNA Sarrah augments recovery from acute myocardial infarction.', 'authors' => 'Trembinski DJ, Bink DI, Theodorou K, Sommer J, Fischer A, van Bergen A, Kuo CC, Costa IG, Schürmann C, Leisegang MS, Brandes RP, Alekseeva T, Brill B, Wietelmann A, Johnson CN, Spring-Connell A, Kaulich M, Werfel S, Engelhardt S, Hirt MN, Yorgan K, Eschen', 'description' => '<p>Long non-coding RNAs (lncRNAs) contribute to cardiac (patho)physiology. Aging is the major risk factor for cardiovascular disease with cardiomyocyte apoptosis as one underlying cause. Here, we report the identification of the aging-regulated lncRNA Sarrah (ENSMUST00000140003) that is anti-apoptotic in cardiomyocytes. Importantly, loss of SARRAH (OXCT1-AS1) in human engineered heart tissue results in impaired contractile force development. SARRAH directly binds to the promoters of genes downregulated after SARRAH silencing via RNA-DNA triple helix formation and cardiomyocytes lacking the triple helix forming domain of Sarrah show an increase in apoptosis. One of the direct SARRAH targets is NRF2, and restoration of NRF2 levels after SARRAH silencing partially rescues the reduction in cell viability. Overexpression of Sarrah in mice shows better recovery of cardiac contractile function after AMI compared to control mice. In summary, we identified the anti-apoptotic evolutionary conserved lncRNA Sarrah, which is downregulated by aging, as a regulator of cardiomyocyte survival.</p>', 'date' => '2020-04-27', 'pmid' => 'http://www.pubmed.gov/32341350', 'doi' => '10.1038/s41467-020-15995-2', 'modified' => '2020-08-17 10:30:19', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '3933', 'name' => 'The endocannabinoid anandamide has an anti-inflammatory effect on CCL2 expression in vascular smooth muscle cells.', 'authors' => 'Pflüger-Müller B, Oo JA, Heering J, Warwick T, Proschak E, Günther S, Looso M, Rezende F, Fork C, Geisslinger G, Thomas D, Gurke R, Steinhilber D, Schulz M, Leisegang MS, Brandes RP', 'description' => '<p>Endocannabinoids are important lipid-signaling mediators. Both protective and deleterious effects of endocannabinoids in the cardiovascular system have been reported but the mechanistic basis for these contradicting observations is unclear. We set out to identify anti-inflammatory mechanisms of endocannabinoids in the murine aorta and in human vascular smooth muscle cells (hVSMC). In response to combined stimulation with cytokines, IL-1β and TNFα, the murine aorta released several endocannabinoids, with anandamide (AEA) levels being the most significantly increased. AEA pretreatment had profound effects on cytokine-induced gene expression in hVSMC and murine aorta. As revealed by RNA-Seq analysis, the induction of a subset of 21 inflammatory target genes, including the important cytokine CCL2 was blocked by AEA. This effect was not mediated through AEA-dependent interference of the AP-1 or NF-κB pathways but rather through an epigenetic mechanism. In the presence of AEA, ATAC-Seq analysis and chromatin-immunoprecipitations revealed that CCL2 induction was blocked due to increased levels of H3K27me3 and a decrease of H3K27ac leading to compacted chromatin structure in the CCL2 promoter. These effects were mediated by recruitment of HDAC4 and the nuclear corepressor NCoR1 to the CCL2 promoter. This study therefore establishes a novel anti-inflammatory mechanism for the endogenous endocannabinoid AEA in vascular smooth muscle cells. Furthermore, this work provides a link between endogenous endocannabinoid signaling and epigenetic regulation.</p>', 'date' => '2020-04-22', 'pmid' => 'http://www.pubmed.gov/32323032', 'doi' => '10.1007/s00395-020-0793-3', 'modified' => '2020-08-17 10:39:12', 'created' => '2020-08-10 12:12:25', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '3407', 'name' => 'The histone demethylase Jarid1b mediates angiotensin II-induced endothelial dysfunction by controlling the 3'UTR of soluble epoxide hydrolase.', 'authors' => 'Vasconez AE, Janetzko P, Oo JA, Pflüger-Müller B, Ratiu C, Gu L, Helin K, Geisslinger G, Fleming I, Schröder K, Fork C, Brandes RP, Leisegang MS', 'description' => '<p>AIM: The histone demethylase Jarid1b limits gene expression by removing the active methyl mark from histone3 lysine4 at gene promoter regions. A vascular function of Jarid1b is unknown, but a vasoprotective function to inflammatory and hypertrophic stimuli, like angiotensin II (AngII) could be inferred. This hypothesis was tested using Jarid1b knockout mice and the inhibitor PBIT. METHODS: Mice or aortic segments were treated with AngII to induce endothelial dysfunction. Aortae from WT and Jarid1b knockout were studied in organ chambers and endothelium-dependent dilator responses to acetylcholine and endothelium-independent responses to DetaNONOate were recorded after pre-constriction with phenylephrine in the presence or absence of the NO-synthase inhibitor nitro-L-arginine. Molecular mechanisms were investigated with chromatin immunoprecipitation, RNA-Seq, RNA-3'-adaptor-ligation, actinomycin D and RNA-immunoprecipitation. RESULTS: Knockout or inhibition of Jarid1b prevented the development of endothelial dysfunction in response to AngII. This effect was not a consequence of altered nitrite oxide availability but accompanied by a loss of the inflammatory response to AngII. As Jarid1b mainly inhibits gene expression, an indirect effect should account for this observation. AngII induced the soluble epoxide hydrolase (sEH), which degrades anti-inflammatory lipids, and thus promotes inflammation. Knockout or inhibition of Jarid1b prevented the AngII-mediated sEH induction. Mechanistically, Jarid1b maintained the length of the 3'untranslated region of the sEH mRNA, thereby increasing its stability and thus sEH protein expression. Loss of Jarid1b activity therefore resulted in sEH mRNA destabilization. CONCLUSION: Jarid1b contributes to the pro-inflammatory effects of AngII by stabilizing sEH expression. Jarid1b inhibition might be an option for future therapeutics against cardiovascular dysfunction.</p>', 'date' => '2018-08-04', 'pmid' => 'http://www.pubmed.gov/30076673', 'doi' => '10.1111/apha.13168', 'modified' => '2018-11-09 11:18:29', 'created' => '2018-11-08 12:59:45', 'ProductsPublication' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( [maximum depth reached] ) ) ), 'Testimonial' => array(), 'Area' => array(), 'SafetySheet' => array( (int) 0 => array( 'id' => '864', 'name' => 'Proteinase K SDS US en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-US-en-GHS_1_0.pdf', 'countries' => 'US', 'modified' => '2020-09-22 14:21:25', 'created' => '2020-09-22 14:21:25', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 1 => array( 'id' => '862', 'name' => 'Proteinase K SDS GB en', 'language' => 'en', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-GB-en-GHS_1_0.pdf', 'countries' => 'GB', 'modified' => '2020-09-22 14:20:24', 'created' => '2020-09-22 14:20:24', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 2 => array( 'id' => '857', 'name' => 'Proteinase K SDS BE fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-fr-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:02', 'created' => '2020-09-22 14:18:02', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 3 => array( 'id' => '861', 'name' => 'Proteinase K SDS FR fr', 'language' => 'fr', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-FR-fr-GHS_1_0.pdf', 'countries' => 'FR', 'modified' => '2020-09-22 14:19:56', 'created' => '2020-09-22 14:19:56', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 4 => array( 'id' => '860', 'name' => 'Proteinase K SDS ES es', 'language' => 'es', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-ES-es-GHS_1_0.pdf', 'countries' => 'ES', 'modified' => '2020-09-22 14:19:27', 'created' => '2020-09-22 14:19:27', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 5 => array( 'id' => '859', 'name' => 'Proteinase K SDS DE de', 'language' => 'de', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-DE-de-GHS_1_0.pdf', 'countries' => 'DE', 'modified' => '2020-09-22 14:18:55', 'created' => '2020-09-22 14:18:55', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 6 => array( 'id' => '863', 'name' => 'Proteinase K SDS JP ja', 'language' => 'ja', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-JP-ja-GHS_1_0.pdf', 'countries' => 'JP', 'modified' => '2020-09-22 14:20:54', 'created' => '2020-09-22 14:20:54', 'ProductsSafetySheet' => array( [maximum depth reached] ) ), (int) 7 => array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( [maximum depth reached] ) ) ) ) $country = 'US' $countries_allowed = array( (int) 0 => 'CA', (int) 1 => 'US', (int) 2 => 'IE', (int) 3 => 'GB', (int) 4 => 'DK', (int) 5 => 'NO', (int) 6 => 'SE', (int) 7 => 'FI', (int) 8 => 'NL', (int) 9 => 'BE', (int) 10 => 'LU', (int) 11 => 'FR', (int) 12 => 'DE', (int) 13 => 'CH', (int) 14 => 'AT', (int) 15 => 'ES', (int) 16 => 'IT', (int) 17 => 'PT' ) $outsource = false $other_formats = array() $edit = '' $testimonials = '' $featured_testimonials = '' $related_products = '' $rrbs_service = array( (int) 0 => (int) 1894, (int) 1 => (int) 1895 ) $chipseq_service = array( (int) 0 => (int) 2683, (int) 1 => (int) 1835, (int) 2 => (int) 1836, (int) 3 => (int) 2684, (int) 4 => (int) 1838, (int) 5 => (int) 1839, (int) 6 => (int) 1856 ) $labelize = object(Closure) { } $old_catalog_number = '<br/><small><span style="color:#CCC">(kch-507-100)</span></small>' $country_code = 'US' $label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>' $protocol = array( 'id' => '10', 'name' => 'FFPE DNA extraction protocol using the Bioruptor®', 'description' => '<p><span>The number of archival formalin-fixed paraffin embedded (FFPE) samples is in the millions, providing an invaluable repository of information for genetic analysis. These samples can be analyzed for a wealth of applications including biomarker discovery, drug development, and cancer research. </span><span>Diagenode’s FFPE DNA Extraction kit is optimized for the extraction of DNA from FFPE tissue sections in conjunction with the Bioruptor</span><span>®</span><span>. </span></p>', 'image_id' => '204', 'type' => 'Protocol', 'url' => 'files/protocols/FFPE_DNA_extraction_protocol.pdf', 'slug' => 'ffpe-dna-extraction-protocol', 'meta_keywords' => '', 'meta_description' => '', 'modified' => '2016-04-29 17:42:46', 'created' => '2015-07-20 10:35:07', 'ProductsProtocol' => array( 'id' => '51', 'product_id' => '1934', 'protocol_id' => '10' ) ) $document = array( 'id' => '136', 'name' => 'Datasheet ProteinaseK kch-507-100', 'description' => 'Datasheet description', 'image_id' => null, 'type' => 'Datasheet', 'url' => 'files/products/reagents/Datasheet_ProteinaseK_kch-507-100.pdf', 'slug' => 'datasheet-proteinasek-kch-507-100', 'meta_keywords' => null, 'meta_description' => null, 'modified' => '2015-07-07 11:47:43', 'created' => '2015-07-07 11:47:43', 'ProductsDocument' => array( 'id' => '886', 'product_id' => '1934', 'document_id' => '136' ) ) $sds = array( 'id' => '858', 'name' => 'Proteinase K SDS BE nl', 'language' => 'nl', 'url' => 'files/SDS/K/SDS-C06050001_2-proteinase_K-BE-nl-GHS_1_0.pdf', 'countries' => 'BE', 'modified' => '2020-09-22 14:18:29', 'created' => '2020-09-22 14:18:29', 'ProductsSafetySheet' => array( 'id' => '1538', 'product_id' => '1934', 'safety_sheet_id' => '858' ) ) $publication = array( 'id' => '3541', 'name' => 'Long noncoding RNA LISPR1 is required for S1P signaling and endothelial cell function.', 'authors' => 'Josipovic I, Pflüger B, Fork C, Vasconez AE, Oo JA, Hitzel J, Seredinski S, Gamen E, Heringdorf DMZ, Chen W, Looso M, Pullamsetti SS, Brandes RP, Leisegang MS', 'description' => '<p>Sphingosine-1-Phosphate (S1P) is a potent signaling lipid. The effects of S1P are mediated by the five S1P receptors (S1PR). In the endothelium S1PR1 is the predominant receptor and thus S1PR1 abundance limits S1P signaling. Recently, lncRNAs were identified as a novel class of molecules regulating gene expression. Interestingly, the lncRNA NONHSAT004848 (LISPR1, Long intergenic noncoding RNA antisense to S1PR1), is closely positioned to the S1P1 receptors gene and in part shares its promoter region. We hypothesize that LISPR1 controls endothelial S1PR1 expression and thus S1P-induced signaling in endothelial cells. In vitro transcription and translation as well as coding potential assessment showed that LISPR1 is indeed noncoding. LISPR1 was localized in both cytoplasm and nucleus and harbored a PolyA tail at the 3'end. In human umbilical vein endothelial cells, as well as human lung tissue, qRT-PCR and RNA-Seq revealed high expression of LISPR1. S1PR1 and LISPR1 were downregulated in human pulmonary diseases such as COPD. LISPR1 but also S1PR1 were induced by inflammation, shear stress and statins. Knockdown of LISPR1 attenuated endothelial S1P-induced migration and spheroid outgrowth of endothelial cells. LISPR1 knockdown decreased S1PR1 expression, which was paralleled by an increase of the binding of the transcriptional repressor ZNF354C to the S1PR1 promoter and a reduction of the recruitment of RNA Polymerase II to the S1PR1 5'end. This resulted in attenuated S1PR1 expression and attenuated S1P downstream signaling. Collectively, the disease relevant lncRNA LISPR1 acts as a novel regulatory unit important for S1PR1 expression and endothelial cell function.</p>', 'date' => '2018-03-01', 'pmid' => 'http://www.pubmed.gov/29408197', 'doi' => '10.1016/j.yjmcc.2018.01.015', 'modified' => '2019-02-28 10:52:59', 'created' => '2019-02-27 12:54:44', 'ProductsPublication' => array( 'id' => '3292', 'product_id' => '1934', 'publication_id' => '3541' ) ) $externalLink = ' <a href="http://www.pubmed.gov/29408197" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755 View::_evaluate() - CORE/Cake/View/View.php, line 971 View::_render() - CORE/Cake/View/View.php, line 933 View::render() - CORE/Cake/View/View.php, line 473 Controller::render() - CORE/Cake/Controller/Controller.php, line 963 ProductsController::slug() - APP/Controller/ProductsController.php, line 1052 ReflectionMethod::invokeArgs() - [internal], line ?? Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491 Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193 Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167 [main] - APP/webroot/index.php, line 118
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