anti b1 integrin subunit antibody Search Results


90
AB Enzymes rohapec® b1 l
Rohapec® B1 L, supplied by AB Enzymes, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson atp synthase b
Atp Synthase B, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
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Becton Dickinson anti-human cd120a mabtnfr1-b1) antibody
Anti Human Cd120a Mabtnfr1 B1) Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
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Becton Dickinson anti-human tcr-gd antibody b1
Anti Human Tcr Gd Antibody B1, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Becton Dickinson cyclin b1
Cyclin B1, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
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Becton Dickinson mouse monoclonal b1 integrin
Mouse Monoclonal B1 Integrin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson anti-γδtcr (apc, b1, mouse igg1
Anti γδtcr (Apc, B1, Mouse Igg1, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson anti-cyclin b1 (554179)
NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of <t>cyclin</t> <t>B1,</t> phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.
Anti Cyclin B1 (554179), supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+b1+integrin+subunit+antibody/anti+cyclin+d1++554180+/pmc05354443-254-17-24
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Becton Dickinson mouse anti-human cyclin b1 antibody (gns-11; 1:500)
NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of <t>cyclin</t> <t>B1,</t> phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.
Mouse Anti Human Cyclin B1 Antibody (Gns 11; 1:500), supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson mouse mab ts2/16
NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of <t>cyclin</t> <t>B1,</t> phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.
Mouse Mab Ts2/16, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Boster Bio aldh1b1 antibody
NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of <t>cyclin</t> <t>B1,</t> phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.
Aldh1b1 Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Bioss boster pb0065 lamin b
NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of <t>cyclin</t> <t>B1,</t> phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.
Boster Pb0065 Lamin B, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of cyclin B1, phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.

Journal: PLoS Pathogens

Article Title: Parvovirus B19 NS1 protein induces cell cycle arrest at G2-phase by activating the ATR-CDC25C-CDK1 pathway

doi: 10.1371/journal.ppat.1006266

Figure Lengend Snippet: NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox (5 μg/ml) and collected and lysed 72 h later. (A) Cell lysates were analyzed for expression of cyclin B1, phosphorylated CDK1 (CDK1(pY15) and CDK1(pT161), lower band ), and total CDK1 by Western blotting. (B) Cell lysates were analyzed for expression of ATM(pS1981), ATM, CHK2, CHK2(pS33/35), and β-actin by Western blotting. (C) Cell lysates were analyzed for expression of p21 by Western blotting with an anti-p21 antibody. β-actin was used as a loading control. Untreated UT7/Epo-S1 (S1) cells, S1 cells treated with nocodazole (Noco), and S1 cells treated with hydroxyurea (HU) were used as controls.

Article Snippet: The following first antibodies were purchased: anti-Strep (A01732) from GenScript, Piscataway, NJ; mouse anti-BrdU (clone B44) (347580), anti-cyclin B1 (554179), anti-CDK1 (pY15) (612306) from BD, San Jose, CA; rabbit anti-BrdU (600-401-C29) and mouse anti-Flag (2001-301-1313) from Rockland, Limerick, PA; anti-CDK1 (A303-663A), anti-CDC25C (A301-390A), anti-MYT1 (A302-424A), anti-p38 (A300-707A) from Bethyl, Montgomery, TX; anti-CDK1 (pT161) (P12-1090) from Assay Biotech, Sunnyvale, CA; anti-CDC25C(pS216) (4204), anti-γH2AX(pS139) (05–636), anti-B19V capsid (MAB8292) from Millipore, Billerica, MA; anti-WEE1 (AP8106b), anti-CHK1 (AM7401a), anti-CHK2 (AP4999a), anti-MAPKAPK2(pS272) (AP3147a) from Abgent, San Diego, CA; anti-ATR (ab2905), anti-GAPDH (Ab8245) from Abcam, Cambridge, MA; anti-ATR (pT1989) (GTX128145), anti-CHK1(pS345) (GTX100065S), anti-RPA32(pT21) (GTX62664) from GeneTex, Irvine, CA; anti-ATM (2873), anti-MAPKAPK2(MK2) (12155s), anti-MARK3 (9311s), anti-p21 (2947p), anti-Histone H3 (9715S) from Cell Signaling Technology, Danvers, MA; anti-ATM(pS1981) (2952–1), anti-CHK2(pS33/35) (2297–1) from Epitomics, Burlingame, CA; anti-p38 (pT180/Y182) (p190-1802) from Phosphosolutions, Aurora, CO; anti-β-actin (A5441) from Sigma-Aldrich, St. Louis, MO.

Techniques: Expressing, Western Blot

(A) Western blot analysis. NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox for 72 h, collected, and lysed, and the nuclei were extracted. Western blot analysis was then performed to detect cyclin B1 and phosphorylated CDK1(pY15), as well as nuclear histone H3 and cytoplasmic GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase). Nuclear extracts from S1 cells and S1 cells treated with nocodazole (Noco) were loaded as controls. (B&C) In vitro CDK1 kinase assay. Equivalent amounts of proteins derived from whole cell lysate (B) or nuclear extracts (C) from S1 cells, S1 cells treated with Noco, and Dox-induced NS1-S1 and NS1 mTAD2 -S1 cells were immunoprecipitated with anti-cyclin B1-crosslinked protein A/G Plus agarose beads for in vitro CDK1 kinase assay. The final products were resolved on a 12% SDS-polyacrylamide gel. The gel was then dried prior to autoradiography, and the phosphorylated histone H1 (pHistone H1) is indicated. (C) Lower panel: Co-Immunoprecipitation (Co-IP) of cyclin B1 and CDK1(pY15) in the nuclear extracts. Nuclear extracts prepared from S1, S1/Noco, NS1-S1/Dox+, and NS1 mTAD2 -S1/Dox+ cells were immunoprecipitated with an anti-cyclin B1 antibody. The eluted proteins were analyzed for CDK1(pY15) by Western blotting. Normal mouse IgG (IgG Ctrl) was used as negative control of immunoprecipitation of control S1 cell extracts.

Journal: PLoS Pathogens

Article Title: Parvovirus B19 NS1 protein induces cell cycle arrest at G2-phase by activating the ATR-CDC25C-CDK1 pathway

doi: 10.1371/journal.ppat.1006266

Figure Lengend Snippet: (A) Western blot analysis. NS1-S1 and NS1 mTAD2 -S1 cells were treated with Dox for 72 h, collected, and lysed, and the nuclei were extracted. Western blot analysis was then performed to detect cyclin B1 and phosphorylated CDK1(pY15), as well as nuclear histone H3 and cytoplasmic GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase). Nuclear extracts from S1 cells and S1 cells treated with nocodazole (Noco) were loaded as controls. (B&C) In vitro CDK1 kinase assay. Equivalent amounts of proteins derived from whole cell lysate (B) or nuclear extracts (C) from S1 cells, S1 cells treated with Noco, and Dox-induced NS1-S1 and NS1 mTAD2 -S1 cells were immunoprecipitated with anti-cyclin B1-crosslinked protein A/G Plus agarose beads for in vitro CDK1 kinase assay. The final products were resolved on a 12% SDS-polyacrylamide gel. The gel was then dried prior to autoradiography, and the phosphorylated histone H1 (pHistone H1) is indicated. (C) Lower panel: Co-Immunoprecipitation (Co-IP) of cyclin B1 and CDK1(pY15) in the nuclear extracts. Nuclear extracts prepared from S1, S1/Noco, NS1-S1/Dox+, and NS1 mTAD2 -S1/Dox+ cells were immunoprecipitated with an anti-cyclin B1 antibody. The eluted proteins were analyzed for CDK1(pY15) by Western blotting. Normal mouse IgG (IgG Ctrl) was used as negative control of immunoprecipitation of control S1 cell extracts.

Article Snippet: The following first antibodies were purchased: anti-Strep (A01732) from GenScript, Piscataway, NJ; mouse anti-BrdU (clone B44) (347580), anti-cyclin B1 (554179), anti-CDK1 (pY15) (612306) from BD, San Jose, CA; rabbit anti-BrdU (600-401-C29) and mouse anti-Flag (2001-301-1313) from Rockland, Limerick, PA; anti-CDK1 (A303-663A), anti-CDC25C (A301-390A), anti-MYT1 (A302-424A), anti-p38 (A300-707A) from Bethyl, Montgomery, TX; anti-CDK1 (pT161) (P12-1090) from Assay Biotech, Sunnyvale, CA; anti-CDC25C(pS216) (4204), anti-γH2AX(pS139) (05–636), anti-B19V capsid (MAB8292) from Millipore, Billerica, MA; anti-WEE1 (AP8106b), anti-CHK1 (AM7401a), anti-CHK2 (AP4999a), anti-MAPKAPK2(pS272) (AP3147a) from Abgent, San Diego, CA; anti-ATR (ab2905), anti-GAPDH (Ab8245) from Abcam, Cambridge, MA; anti-ATR (pT1989) (GTX128145), anti-CHK1(pS345) (GTX100065S), anti-RPA32(pT21) (GTX62664) from GeneTex, Irvine, CA; anti-ATM (2873), anti-MAPKAPK2(MK2) (12155s), anti-MARK3 (9311s), anti-p21 (2947p), anti-Histone H3 (9715S) from Cell Signaling Technology, Danvers, MA; anti-ATM(pS1981) (2952–1), anti-CHK2(pS33/35) (2297–1) from Epitomics, Burlingame, CA; anti-p38 (pT180/Y182) (p190-1802) from Phosphosolutions, Aurora, CO; anti-β-actin (A5441) from Sigma-Aldrich, St. Louis, MO.

Techniques: Western Blot, In Vitro, Kinase Assay, Derivative Assay, Immunoprecipitation, Autoradiography, Co-Immunoprecipitation Assay, Negative Control

NS1 activates ATR through its TAD domain. Activated ATR then transduces signals to CDC25C through activating CHK1. CDC25C phosphatase activity is negatively regulated by phosphorylation at serine 216, which then creates a binding site for the 14-3-3 protein in the cytoplasm . Thus, inactive CDC25C cannot dephosphorylate the cyclin B1/CDK1(pT14/Y15) complex; the latter component is inactive, and so progression from G2- to M-phase is blocked. It is proposed that DNA replication-induced DDR, and thereafter ATR/CHK1 activation, which plays a role in viral DNA replication, should not be involved in CDC25C phosphorylation (see the section for further explanation). The question mark indicates potential modification of CHK1, in addition to the phosphorylation at S345.

Journal: PLoS Pathogens

Article Title: Parvovirus B19 NS1 protein induces cell cycle arrest at G2-phase by activating the ATR-CDC25C-CDK1 pathway

doi: 10.1371/journal.ppat.1006266

Figure Lengend Snippet: NS1 activates ATR through its TAD domain. Activated ATR then transduces signals to CDC25C through activating CHK1. CDC25C phosphatase activity is negatively regulated by phosphorylation at serine 216, which then creates a binding site for the 14-3-3 protein in the cytoplasm . Thus, inactive CDC25C cannot dephosphorylate the cyclin B1/CDK1(pT14/Y15) complex; the latter component is inactive, and so progression from G2- to M-phase is blocked. It is proposed that DNA replication-induced DDR, and thereafter ATR/CHK1 activation, which plays a role in viral DNA replication, should not be involved in CDC25C phosphorylation (see the section for further explanation). The question mark indicates potential modification of CHK1, in addition to the phosphorylation at S345.

Article Snippet: The following first antibodies were purchased: anti-Strep (A01732) from GenScript, Piscataway, NJ; mouse anti-BrdU (clone B44) (347580), anti-cyclin B1 (554179), anti-CDK1 (pY15) (612306) from BD, San Jose, CA; rabbit anti-BrdU (600-401-C29) and mouse anti-Flag (2001-301-1313) from Rockland, Limerick, PA; anti-CDK1 (A303-663A), anti-CDC25C (A301-390A), anti-MYT1 (A302-424A), anti-p38 (A300-707A) from Bethyl, Montgomery, TX; anti-CDK1 (pT161) (P12-1090) from Assay Biotech, Sunnyvale, CA; anti-CDC25C(pS216) (4204), anti-γH2AX(pS139) (05–636), anti-B19V capsid (MAB8292) from Millipore, Billerica, MA; anti-WEE1 (AP8106b), anti-CHK1 (AM7401a), anti-CHK2 (AP4999a), anti-MAPKAPK2(pS272) (AP3147a) from Abgent, San Diego, CA; anti-ATR (ab2905), anti-GAPDH (Ab8245) from Abcam, Cambridge, MA; anti-ATR (pT1989) (GTX128145), anti-CHK1(pS345) (GTX100065S), anti-RPA32(pT21) (GTX62664) from GeneTex, Irvine, CA; anti-ATM (2873), anti-MAPKAPK2(MK2) (12155s), anti-MARK3 (9311s), anti-p21 (2947p), anti-Histone H3 (9715S) from Cell Signaling Technology, Danvers, MA; anti-ATM(pS1981) (2952–1), anti-CHK2(pS33/35) (2297–1) from Epitomics, Burlingame, CA; anti-p38 (pT180/Y182) (p190-1802) from Phosphosolutions, Aurora, CO; anti-β-actin (A5441) from Sigma-Aldrich, St. Louis, MO.

Techniques: Activity Assay, Binding Assay, Activation Assay, Modification