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goat anti human polyclonal reck antibody  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology goat anti human polyclonal reck antibody
    Goat Anti Human Polyclonal Reck Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+reck/RECK+Antibody/pmc07136997-93-4-9
    Average 93 stars, based on 45 article reviews
    goat anti human polyclonal reck antibody - by Bioz Stars, 2026-11
    93/100 stars

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    Related Articles

    other:

    Article Title: Wnt7 variants capable of activating g-protein coupled receptor (Gpr)124/Reck/frizzled/lipoprotein receptor-related protein (LRP)-mediated Wnt signaling
    Article Snippet: Non-limiting examples of RECK antibodies include antibodies which are known in the art and commercially available, such as from Abcam (e.g. ab88249 and ab89915 specific for human full-length RECK), Cell Signaling Technology (e.g. #3433 specific for human, mouse, rat, monkey RECK (D8C7)), Santa Cruz (e.g. sc-373929 specific for C-terminus of human RECK).

    Article Title: Casticin inhibits the activity of transcription factor Sp1 and the methylation of RECK in MGC803 gastric cancer cells
    Article Snippet: A total of 80 μg protein was resolved using 12% SDS-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose membranes (Sigma-Aldrich; Merck Millipore) under 30 V at 4°C.

    Immunohistochemical staining:

    Article Title: Low expression of RECK in oral squamous cell carcinoma patients induces a shorter survival rate through an imbalance of RECK/MMPs
    Article Snippet: .. Immunohistochemical reagents include the goat anti-human polyclonal RECK antibody (Santa Cruz, 1:75) and the mouse anti-human monoclonal MMP-2 and MMP-9 antibodies (Boshide, China, 1:100). ..

    shRNA:

    Article Title: Preeclampsia associates with RECK-dependent decrease in human trophoblasts migration and invasion.
    Article Snippet: Introduction.. Preeclampsia is characterized by reduced invasion capacity of trophoblasts involving lower matrix metalloproteinase (MMP) activity.. Cell invasion is reduced by reversion-inducing-cysteine-rich protein with Kazal motifs (RECK), a plasma membrane protein that inhibits MMP in several cell types.

    Plasmid Preparation:

    Article Title: Preeclampsia associates with RECK-dependent decrease in human trophoblasts migration and invasion.
    Article Snippet: Introduction.. Preeclampsia is characterized by reduced invasion capacity of trophoblasts involving lower matrix metalloproteinase (MMP) activity.. Cell invasion is reduced by reversion-inducing-cysteine-rich protein with Kazal motifs (RECK), a plasma membrane protein that inhibits MMP in several cell types.

    Transfection:

    Article Title: Preeclampsia associates with RECK-dependent decrease in human trophoblasts migration and invasion.
    Article Snippet: Introduction.. Preeclampsia is characterized by reduced invasion capacity of trophoblasts involving lower matrix metalloproteinase (MMP) activity.. Cell invasion is reduced by reversion-inducing-cysteine-rich protein with Kazal motifs (RECK), a plasma membrane protein that inhibits MMP in several cell types.

    Blocking Assay:

    Article Title: Casticin inhibits the activity of transcription factor Sp1 and the methylation of RECK in MGC803 gastric cancer cells
    Article Snippet: A total of 80 µg protein was resolved using 12% SDS-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose membranes (Sigma-Aldrich; Merck Millipore) under 30 V at 4°C. .. Following blocking at 4°C and washing with Tris-buffered saline with Tween-20 (TBST) for 30 min, the membranes were incubated with polyclonal rabbit anti-human RECK (1:400; sc-28918) or DNMT1 antibodies (1:400; sc-20701) or rabbit anti-β-actin antibodies (1:1,000; sc-7210; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA) at 4°C for 8 h. After washing with TBST for 30 min, the membrane was incubated with horseradish peroxidase (HRP)-labeled goat anti-rabbit immunoglobulin G antibody (1:5,000; sc-2054; Santa Cruz Biotechnology, Inc.) for 4 h at room temperature. .. Following treatment with casticin, MGC803 cells (1×10 7 ) underwent genomic DNA extraction and purification using the DNeasy Blood & Tissue kit (Qiagen GmbH, Hilden, Germany).

    Saline:

    Article Title: Casticin inhibits the activity of transcription factor Sp1 and the methylation of RECK in MGC803 gastric cancer cells
    Article Snippet: A total of 80 µg protein was resolved using 12% SDS-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose membranes (Sigma-Aldrich; Merck Millipore) under 30 V at 4°C. .. Following blocking at 4°C and washing with Tris-buffered saline with Tween-20 (TBST) for 30 min, the membranes were incubated with polyclonal rabbit anti-human RECK (1:400; sc-28918) or DNMT1 antibodies (1:400; sc-20701) or rabbit anti-β-actin antibodies (1:1,000; sc-7210; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA) at 4°C for 8 h. After washing with TBST for 30 min, the membrane was incubated with horseradish peroxidase (HRP)-labeled goat anti-rabbit immunoglobulin G antibody (1:5,000; sc-2054; Santa Cruz Biotechnology, Inc.) for 4 h at room temperature. .. Following treatment with casticin, MGC803 cells (1×10 7 ) underwent genomic DNA extraction and purification using the DNeasy Blood & Tissue kit (Qiagen GmbH, Hilden, Germany).

    Incubation:

    Article Title: Casticin inhibits the activity of transcription factor Sp1 and the methylation of RECK in MGC803 gastric cancer cells
    Article Snippet: A total of 80 µg protein was resolved using 12% SDS-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose membranes (Sigma-Aldrich; Merck Millipore) under 30 V at 4°C. .. Following blocking at 4°C and washing with Tris-buffered saline with Tween-20 (TBST) for 30 min, the membranes were incubated with polyclonal rabbit anti-human RECK (1:400; sc-28918) or DNMT1 antibodies (1:400; sc-20701) or rabbit anti-β-actin antibodies (1:1,000; sc-7210; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA) at 4°C for 8 h. After washing with TBST for 30 min, the membrane was incubated with horseradish peroxidase (HRP)-labeled goat anti-rabbit immunoglobulin G antibody (1:5,000; sc-2054; Santa Cruz Biotechnology, Inc.) for 4 h at room temperature. .. Following treatment with casticin, MGC803 cells (1×10 7 ) underwent genomic DNA extraction and purification using the DNeasy Blood & Tissue kit (Qiagen GmbH, Hilden, Germany).

    Membrane:

    Article Title: Casticin inhibits the activity of transcription factor Sp1 and the methylation of RECK in MGC803 gastric cancer cells
    Article Snippet: A total of 80 µg protein was resolved using 12% SDS-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose membranes (Sigma-Aldrich; Merck Millipore) under 30 V at 4°C. .. Following blocking at 4°C and washing with Tris-buffered saline with Tween-20 (TBST) for 30 min, the membranes were incubated with polyclonal rabbit anti-human RECK (1:400; sc-28918) or DNMT1 antibodies (1:400; sc-20701) or rabbit anti-β-actin antibodies (1:1,000; sc-7210; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA) at 4°C for 8 h. After washing with TBST for 30 min, the membrane was incubated with horseradish peroxidase (HRP)-labeled goat anti-rabbit immunoglobulin G antibody (1:5,000; sc-2054; Santa Cruz Biotechnology, Inc.) for 4 h at room temperature. .. Following treatment with casticin, MGC803 cells (1×10 7 ) underwent genomic DNA extraction and purification using the DNeasy Blood & Tissue kit (Qiagen GmbH, Hilden, Germany).



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    Targeting TRAF3IP2 or <t>RECK</t> overexpression blunts IL-18-induced ASMC proliferation and migration. ( A – E ) Silencing TRAF3IP2 inhibits IL-18-induced ASMC proliferation ( B ) and migration ( C ). ASMC were transduced with adenovirus-expressing shRNA targeting human TRAF3IP2 (moi 10 for 48 h), made quiescent, and then exposed to IL-18 (10 ng/mL; experimental design in ( A )). ASMC proliferation was assessed after 48 h of IL-18 addition using the CyQUANT Cell proliferation assay ( B ), and migration after 18 h using Boyden chamber assay ( C ). ASMCs migrating to the lower surface of the membrane were counted in 10 different fields and summarized as mean ± SEM. ( B , C ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6). Knockdown of TRAF3IP2 was confirmed by RT-qPCR using a TaqMan™ probe ( D ) and Western blotting ( E ). ( D , E ) * p < 0.01 vs. untreated (n = 3). ( F , G ) Dose-dependent effects of Ad.RECK on RECK expression (experimental design in ( F )). Induction of RECK following adenoviral transduction was confirmed by Western blotting with tubulin serving as an internal control ( G ). ( H – K ) Forced expression of RECK inhibits IL-18-stimulated ASMC proliferation and migration. ASMCs were transduced with adenovirus-expressing human RECK <t>cDNA</t> (moi 10 for 24 h), made quiescent, and then treated with IL-18 (experimental design in ( H )) and analyzed for proliferation ( I ) and migration ( J ) as in ( B , C ). ( C , J ) The insets show representative images of Matrigel™ Transwell invasion. Scale bar: 20 μM. ( E , G , K ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three ( E ), four ( G ) and three ( K ) independent experiments were semiquantified by densitometry and are summarized on the right. ( I ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6); ( J ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 4); ( K ) * p < 0.01 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).
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    goat anti human polyclonal reck antibody  (Santa Cruz Biotechnology)
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    Santa Cruz Biotechnology goat anti human polyclonal reck antibody
    Targeting TRAF3IP2 or <t>RECK</t> overexpression blunts IL-18-induced ASMC proliferation and migration. ( A – E ) Silencing TRAF3IP2 inhibits IL-18-induced ASMC proliferation ( B ) and migration ( C ). ASMC were transduced with adenovirus-expressing shRNA targeting human TRAF3IP2 (moi 10 for 48 h), made quiescent, and then exposed to IL-18 (10 ng/mL; experimental design in ( A )). ASMC proliferation was assessed after 48 h of IL-18 addition using the CyQUANT Cell proliferation assay ( B ), and migration after 18 h using Boyden chamber assay ( C ). ASMCs migrating to the lower surface of the membrane were counted in 10 different fields and summarized as mean ± SEM. ( B , C ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6). Knockdown of TRAF3IP2 was confirmed by RT-qPCR using a TaqMan™ probe ( D ) and Western blotting ( E ). ( D , E ) * p < 0.01 vs. untreated (n = 3). ( F , G ) Dose-dependent effects of Ad.RECK on RECK expression (experimental design in ( F )). Induction of RECK following adenoviral transduction was confirmed by Western blotting with tubulin serving as an internal control ( G ). ( H – K ) Forced expression of RECK inhibits IL-18-stimulated ASMC proliferation and migration. ASMCs were transduced with adenovirus-expressing human RECK <t>cDNA</t> (moi 10 for 24 h), made quiescent, and then treated with IL-18 (experimental design in ( H )) and analyzed for proliferation ( I ) and migration ( J ) as in ( B , C ). ( C , J ) The insets show representative images of Matrigel™ Transwell invasion. Scale bar: 20 μM. ( E , G , K ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three ( E ), four ( G ) and three ( K ) independent experiments were semiquantified by densitometry and are summarized on the right. ( I ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6); ( J ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 4); ( K ) * p < 0.01 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).
    Goat Anti Human Polyclonal Reck Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+reck/RECK+Antibody/pmc07136997-93-4-9
    Average 93 stars, based on 1 article reviews
    goat anti human polyclonal reck antibody - by Bioz Stars, 2026-11
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Targeting TRAF3IP2 or RECK overexpression blunts IL-18-induced ASMC proliferation and migration. ( A – E ) Silencing TRAF3IP2 inhibits IL-18-induced ASMC proliferation ( B ) and migration ( C ). ASMC were transduced with adenovirus-expressing shRNA targeting human TRAF3IP2 (moi 10 for 48 h), made quiescent, and then exposed to IL-18 (10 ng/mL; experimental design in ( A )). ASMC proliferation was assessed after 48 h of IL-18 addition using the CyQUANT Cell proliferation assay ( B ), and migration after 18 h using Boyden chamber assay ( C ). ASMCs migrating to the lower surface of the membrane were counted in 10 different fields and summarized as mean ± SEM. ( B , C ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6). Knockdown of TRAF3IP2 was confirmed by RT-qPCR using a TaqMan™ probe ( D ) and Western blotting ( E ). ( D , E ) * p < 0.01 vs. untreated (n = 3). ( F , G ) Dose-dependent effects of Ad.RECK on RECK expression (experimental design in ( F )). Induction of RECK following adenoviral transduction was confirmed by Western blotting with tubulin serving as an internal control ( G ). ( H – K ) Forced expression of RECK inhibits IL-18-stimulated ASMC proliferation and migration. ASMCs were transduced with adenovirus-expressing human RECK cDNA (moi 10 for 24 h), made quiescent, and then treated with IL-18 (experimental design in ( H )) and analyzed for proliferation ( I ) and migration ( J ) as in ( B , C ). ( C , J ) The insets show representative images of Matrigel™ Transwell invasion. Scale bar: 20 μM. ( E , G , K ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three ( E ), four ( G ) and three ( K ) independent experiments were semiquantified by densitometry and are summarized on the right. ( I ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6); ( J ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 4); ( K ) * p < 0.01 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).

    Journal: Cells

    Article Title: EF24, a Curcumin Analog, Reverses Interleukin-18-Induced miR-30a or miR-342-Dependent TRAF3IP2 Expression, RECK Suppression, and the Proinflammatory Phenotype of Human Aortic Smooth Muscle Cells

    doi: 10.3390/cells13201673

    Figure Lengend Snippet: Targeting TRAF3IP2 or RECK overexpression blunts IL-18-induced ASMC proliferation and migration. ( A – E ) Silencing TRAF3IP2 inhibits IL-18-induced ASMC proliferation ( B ) and migration ( C ). ASMC were transduced with adenovirus-expressing shRNA targeting human TRAF3IP2 (moi 10 for 48 h), made quiescent, and then exposed to IL-18 (10 ng/mL; experimental design in ( A )). ASMC proliferation was assessed after 48 h of IL-18 addition using the CyQUANT Cell proliferation assay ( B ), and migration after 18 h using Boyden chamber assay ( C ). ASMCs migrating to the lower surface of the membrane were counted in 10 different fields and summarized as mean ± SEM. ( B , C ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6). Knockdown of TRAF3IP2 was confirmed by RT-qPCR using a TaqMan™ probe ( D ) and Western blotting ( E ). ( D , E ) * p < 0.01 vs. untreated (n = 3). ( F , G ) Dose-dependent effects of Ad.RECK on RECK expression (experimental design in ( F )). Induction of RECK following adenoviral transduction was confirmed by Western blotting with tubulin serving as an internal control ( G ). ( H – K ) Forced expression of RECK inhibits IL-18-stimulated ASMC proliferation and migration. ASMCs were transduced with adenovirus-expressing human RECK cDNA (moi 10 for 24 h), made quiescent, and then treated with IL-18 (experimental design in ( H )) and analyzed for proliferation ( I ) and migration ( J ) as in ( B , C ). ( C , J ) The insets show representative images of Matrigel™ Transwell invasion. Scale bar: 20 μM. ( E , G , K ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three ( E ), four ( G ) and three ( K ) independent experiments were semiquantified by densitometry and are summarized on the right. ( I ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+GFP (n = 6); ( J ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 4); ( K ) * p < 0.01 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).

    Article Snippet: Adenoviral vector-expressing human RECK cDNA (GenBank accession # NM_021111) was also custom-generated at Vector Biolabs.

    Techniques: Over Expression, Migration, Transduction, Expressing, shRNA, CyQUANT Assay, Proliferation Assay, Boyden Chamber Assay, Membrane, Knockdown, Quantitative RT-PCR, Western Blot, Control

    Ectopic expression of RECK blunts IL-18-induced inhibition in the expression of SMC markers and the induction of proinflammatory phenotype markers. ( A – F ) Forced expression of RECK restores IL-18-induced suppression of SMC markers and inhibits the induction of proinflammatory phenotype markers. ASMCs were transduced with adenovirus-expressing human RECK cDNA (moi10 for 24 h), made quiescent, and then treated with IL-18 at 10 ng/mL for 48 h (experimental design in ( A )). The expression levels of SMC markers ACTA2 ( B , C ) and MYH11 ( D , E ) were analyzed by RT-qPCR ( B , D ) and Western blotting ( C , E ). The proinflammatory phenotype markers Galectin 3, Olr1, VCAM, CCL2, IL-6, IL-8, and TNF-α were analyzed by RT-qPCR using TaqMan™ probes ( F ). ( C , E ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three independent experiments were semiquantified by densitometry and are summarized on the right. ( B , D , F ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 5). ( C , E ) * p < 0.05 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).

    Journal: Cells

    Article Title: EF24, a Curcumin Analog, Reverses Interleukin-18-Induced miR-30a or miR-342-Dependent TRAF3IP2 Expression, RECK Suppression, and the Proinflammatory Phenotype of Human Aortic Smooth Muscle Cells

    doi: 10.3390/cells13201673

    Figure Lengend Snippet: Ectopic expression of RECK blunts IL-18-induced inhibition in the expression of SMC markers and the induction of proinflammatory phenotype markers. ( A – F ) Forced expression of RECK restores IL-18-induced suppression of SMC markers and inhibits the induction of proinflammatory phenotype markers. ASMCs were transduced with adenovirus-expressing human RECK cDNA (moi10 for 24 h), made quiescent, and then treated with IL-18 at 10 ng/mL for 48 h (experimental design in ( A )). The expression levels of SMC markers ACTA2 ( B , C ) and MYH11 ( D , E ) were analyzed by RT-qPCR ( B , D ) and Western blotting ( C , E ). The proinflammatory phenotype markers Galectin 3, Olr1, VCAM, CCL2, IL-6, IL-8, and TNF-α were analyzed by RT-qPCR using TaqMan™ probes ( F ). ( C , E ) While a representative immunoblot is shown, the intensities of immunoreactive bands from three independent experiments were semiquantified by densitometry and are summarized on the right. ( B , D , F ) * p < at least 0.01 vs. Untreated; † p < 0.01 vs. IL-18 or IL-18+eGFP (n = 5). ( C , E ) * p < 0.05 vs. Untreated; † p < 0.05 vs. IL-18 or IL-18+eGFP (n = 3).

    Article Snippet: Adenoviral vector-expressing human RECK cDNA (GenBank accession # NM_021111) was also custom-generated at Vector Biolabs.

    Techniques: Expressing, Inhibition, Transduction, Quantitative RT-PCR, Western Blot