癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
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Anti-Troponin I (cardiac) Ser23/24 Antibody
Our Anti-Troponin I (cardiac) Ser23/24 rabbit polyclonal phosphospecific primary antibody from Phosp
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Application 
| WB |
|---|---|
| Primary Accession | P48787 |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 24259 Da |
| Gene ID | 21954 |
|---|---|
| Other Names | 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 |
| Target/Specificity | 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). |
| Dilution | WB~~1:1000 |
| Format | Antigen Affinity Purified from Pooled Serum |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Troponin I (cardiac) Ser23/24 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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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