ser 282 Search Results


1° polyclonal rabbit against phosphorylated serine residue 282 (ser-282) cmybp-c  (Enzo Biochem)
90
Enzo Biochem 1° polyclonal rabbit against phosphorylated serine residue 282 (ser-282) cmybp-c
Interventricular differences of myofilament Ca 2+ -sensitivity and protein phosphorylation in the post-ischemic rat heart. Ca 2+ -sensitivities of the contractile machinery of RV ( A ) and LV ( B ) cardiomyocytes are indicated by the pCa 50 values ( small panels ) derived from normalized active force vs. pCa (–log 10 [Ca 2+ ]) relationships. Cardiac myosin binding protein-C <t>(cMyBP-C)</t> phosphorylation at Ser-282 ( C ) and cardiac Troponin I (cTnI) bis-phosphorylation at Ser-23/24 ( D ) are shown after normalization to actin. Insets: Representative images show Western immunoblots using P-site-specific anti-cMyBP-C and anti-cTnI antibodies (top) and corresponding anti-actin antibodies (bottom; discontinuity of the blots indicates identical samples from parallel experiments with different loading order) at molecular weights of ~150 kDa (cMyBP-C), ~24 kDa (cTnI), and ~42 kDa (actin). Data are shown as mean ± SEM; panels A–B: n = 10–13 cardiomyocyte/3–5 heart/group; panels C–D: n = 4–9 sample/3–5 heart/group. * p < 0.05, ** p < 0.01 HFrEF vs. Sham (same ventricle); ## p < 0.01 RV vs. LV (same group).
1° Polyclonal Rabbit Against Phosphorylated Serine Residue 282 (Ser 282) Cmybp C, supplied by Enzo Biochem, 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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1° polyclonal rabbit against phosphorylated serine residue 282 (ser-282) cmybp-c - by Bioz Stars, 2026-04
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Interventricular differences of myofilament Ca 2+ -sensitivity and protein phosphorylation in the post-ischemic rat heart. Ca 2+ -sensitivities of the contractile machinery of RV ( A ) and LV ( B ) cardiomyocytes are indicated by the pCa 50 values ( small panels ) derived from normalized active force vs. pCa (–log 10 [Ca 2+ ]) relationships. Cardiac myosin binding protein-C (cMyBP-C) phosphorylation at Ser-282 ( C ) and cardiac Troponin I (cTnI) bis-phosphorylation at Ser-23/24 ( D ) are shown after normalization to actin. Insets: Representative images show Western immunoblots using P-site-specific anti-cMyBP-C and anti-cTnI antibodies (top) and corresponding anti-actin antibodies (bottom; discontinuity of the blots indicates identical samples from parallel experiments with different loading order) at molecular weights of ~150 kDa (cMyBP-C), ~24 kDa (cTnI), and ~42 kDa (actin). Data are shown as mean ± SEM; panels A–B: n = 10–13 cardiomyocyte/3–5 heart/group; panels C–D: n = 4–9 sample/3–5 heart/group. * p < 0.05, ** p < 0.01 HFrEF vs. Sham (same ventricle); ## p < 0.01 RV vs. LV (same group).

Journal: Antioxidants

Article Title: Interventricular Differences of Signaling Pathways-Mediated Regulation of Cardiomyocyte Function in Response to High Oxidative Stress in the Post-Ischemic Failing Rat Heart

doi: 10.3390/antiox10060964

Figure Lengend Snippet: Interventricular differences of myofilament Ca 2+ -sensitivity and protein phosphorylation in the post-ischemic rat heart. Ca 2+ -sensitivities of the contractile machinery of RV ( A ) and LV ( B ) cardiomyocytes are indicated by the pCa 50 values ( small panels ) derived from normalized active force vs. pCa (–log 10 [Ca 2+ ]) relationships. Cardiac myosin binding protein-C (cMyBP-C) phosphorylation at Ser-282 ( C ) and cardiac Troponin I (cTnI) bis-phosphorylation at Ser-23/24 ( D ) are shown after normalization to actin. Insets: Representative images show Western immunoblots using P-site-specific anti-cMyBP-C and anti-cTnI antibodies (top) and corresponding anti-actin antibodies (bottom; discontinuity of the blots indicates identical samples from parallel experiments with different loading order) at molecular weights of ~150 kDa (cMyBP-C), ~24 kDa (cTnI), and ~42 kDa (actin). Data are shown as mean ± SEM; panels A–B: n = 10–13 cardiomyocyte/3–5 heart/group; panels C–D: n = 4–9 sample/3–5 heart/group. * p < 0.05, ** p < 0.01 HFrEF vs. Sham (same ventricle); ## p < 0.01 RV vs. LV (same group).

Article Snippet: Membranes were then stained with SYPRO Ruby protein blot stain (Invitrogen; Molecular Probes), washed, and probed appropriately with 1° and 2° antibodies: 1° polyclonal rabbit against phosphorylated serine residue 282 (Ser-282) of cMyBP-C (Enzo Life Sciences; dilution 1:5000), 1° polyclonal rabbit against phosphorylated serine residues 23 and 24 (Ser-23/24) of cardiac Troponin I (cTnI; Abcam; dilution 1:1000), 1° monoclonal mouse against actin (Clone HHF35; DakoCytomation; dilution 1:1000); whereas 2° anti-mouse-POD and anti-rabbit-POD (both from Sigma-Aldrich, St. Louis, MO, USA; dilution 1:40,000) were coupled properly with 1° ones.

Techniques: Derivative Assay, Binding Assay, Western Blot

Overall myofilament protein phosphorylation patterns of the RV and the LV in the post-ischemic rat heart. Collection of contractile protein bands in each group is shown by phosphoprotein and protein gel staining of 4% and 15% gels ( A ). SDS-PAGE indicates 1D polyacrylamide gel electrophoresis; MHC, myosin heavy chain; cMyBP-C, cardiac myosin binding protein-C; Tm, tropomyosin; cTnI, cardiac troponin I; MLC-2, myosin light chain 2. Corresponding representations of optical densities of protein gel staining in the RV ( B ) and the LV ( C ) are given in arbitrary units (a.u.). Phosphorylation of titin ( D ), cMyBP-C ( E ), Tm ( F ), cTnI ( G ), and cMLC-2 ( H ) are shown as phosphoprotein/total protein ratios. Data are shown as mean ± SEM; panel D: n = 23–47 SDS-PAGE/3–5 heart/group; panels E-H: n = 8–20 SDS-PAGE/3–5 heart/group. * p < 0.05 HFrEF vs. Sham (same ventricle); ## p < 0.01 RV vs. LV (same group).

Journal: Antioxidants

Article Title: Interventricular Differences of Signaling Pathways-Mediated Regulation of Cardiomyocyte Function in Response to High Oxidative Stress in the Post-Ischemic Failing Rat Heart

doi: 10.3390/antiox10060964

Figure Lengend Snippet: Overall myofilament protein phosphorylation patterns of the RV and the LV in the post-ischemic rat heart. Collection of contractile protein bands in each group is shown by phosphoprotein and protein gel staining of 4% and 15% gels ( A ). SDS-PAGE indicates 1D polyacrylamide gel electrophoresis; MHC, myosin heavy chain; cMyBP-C, cardiac myosin binding protein-C; Tm, tropomyosin; cTnI, cardiac troponin I; MLC-2, myosin light chain 2. Corresponding representations of optical densities of protein gel staining in the RV ( B ) and the LV ( C ) are given in arbitrary units (a.u.). Phosphorylation of titin ( D ), cMyBP-C ( E ), Tm ( F ), cTnI ( G ), and cMLC-2 ( H ) are shown as phosphoprotein/total protein ratios. Data are shown as mean ± SEM; panel D: n = 23–47 SDS-PAGE/3–5 heart/group; panels E-H: n = 8–20 SDS-PAGE/3–5 heart/group. * p < 0.05 HFrEF vs. Sham (same ventricle); ## p < 0.01 RV vs. LV (same group).

Article Snippet: Membranes were then stained with SYPRO Ruby protein blot stain (Invitrogen; Molecular Probes), washed, and probed appropriately with 1° and 2° antibodies: 1° polyclonal rabbit against phosphorylated serine residue 282 (Ser-282) of cMyBP-C (Enzo Life Sciences; dilution 1:5000), 1° polyclonal rabbit against phosphorylated serine residues 23 and 24 (Ser-23/24) of cardiac Troponin I (cTnI; Abcam; dilution 1:1000), 1° monoclonal mouse against actin (Clone HHF35; DakoCytomation; dilution 1:1000); whereas 2° anti-mouse-POD and anti-rabbit-POD (both from Sigma-Aldrich, St. Louis, MO, USA; dilution 1:40,000) were coupled properly with 1° ones.

Techniques: Staining, SDS Page, Polyacrylamide Gel Electrophoresis, Binding Assay