Troponin I (cardiac) Ser23/24 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) .

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Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser23/24 of mouse troponin 1, cardiac (cTnI), conjugated to keyhole limpet hemocyanin (KLH) .

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.