| Overview |
| bs-70294R |
| Troponin I (cardiac) Ser23/24 Antibody |
| WB |
| Specific for endogenous levels of the ~25 kDa cardiac troponin I protein phosphorylated at Ser23/24. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide. |
| Human, Mouse, Rat |
| Non-Human Primate |
| Specifications |
| Unconjugated |
| Rabbit |
| Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser23/24 of mouse troponin 1, cardiac (cTnI), conjugated to keyhole limpet hemocyanin (KLH). |
| Ser23,24 |
| Polyclonal |
| IgG |
| Lot Dependent |
| Antigen Affinity purification from Pooled whole antiserum |
| 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. |
| Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
| Target |
| 21954 |
| P48787 |
| cardiac muscle antibody, Cardiac troponin I antibody, Cardiac Troponin I antibody, cardiomyopathy dilated 2A (autosomal recessive) antibody, Cardiomyopathy familial hypertrophic 7 included antibody, CMD1FF antibody, CMD2A antibody, CMH7 antibody, cTnI antibody, Familial hypertrophic cardiomyopathy 7 antibody, MGC116817 antibody, RCM1 antibody, Tn1 antibody, Tni antibody, TNN I3 antibody, TNNC 1 antibody, TNNC1 antibody, TNNI3 antibody, TNNI3_HUMAN antibody, Troponin I antibody, Troponin I cardiac antibody, Troponin I cardiac muscle antibody, Troponin I cardiac muscle isoform antibody, Troponin I type 3 cardiac antibody, troponin I cardiac 3 antibody, TroponinI antibody, Troponin I type 3 (cardiac) antibody |
| Troponin I (cTnI) is 1 of 3 subunits, along with troponin C (TnC) and troponin T (TnT) of troponin complex found in cardiac muscle. cTnI binds to actin in thin myofilaments to hold the troponin-tropomyosin complex in place. Phosphorylation of cardiac isoform of TnI at serines 22,23 in the unique amino-terminal end molecule decreases the calcium sensitivity of the sarcomere, promotes calcium dissociation from troponin C and by extension enhances rates of cross-bridge cycling and diastolic relaxation (Noland, Jr. et al., 1995; Noland et al., 1989). In addition, studies using reconstituted fibers and mutational analysis have shown that PKC phosphorylation of TnI (largely at Ser-43) inhibits the actin-cross bridge reaction and reduces the Ca++ dependent actomyosin ATPase rate as well as the calcium sensitivity of force generation (Noland, Jr. and Kuo, 1991). Phosphorylation at Thr-144 (mediated by several PKC isoforms) reduces maximal tension development and cross-bridge cycling rates (Sumandea et al., 2008). Importantly, changes in the phosphorylation at each of these sites have been shown to be stage-specific with regard to cardiac disease progression (Walker et al., 2010). |
| Application Dilution |
| WB |
1:300-5000 |
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