| WB | 咨询技术 | Mouse,Rat |
| IF | 咨询技术 | Mouse,Rat |
| IHC | 1/100-1/300 | Mouse,Rat |
| ICC | 技术咨询 | Mouse,Rat |
| FCM | 咨询技术 | Mouse,Rat |
| Elisa | 1/20000 | Mouse,Rat |
| Aliases | TNNI3; TNNC1; Troponin I; cardiac muscle; Cardiac troponin I |
| WB Predicted band size | 28kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Mouse,Rat |
| Immunogen | Synthesized peptide derived from human Troponin I-C around the phosphorylation site of S22/S23. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于Troponin I-C (Phospho-Ser22/Ser23)抗体的3篇参考文献示例(注：文献为虚拟示例，实际需根据真实文献调整)：
1. **文献名称**：*"Phosphorylation of cardiac troponin I at Ser22/23 regulates myocardial function in ischemia-reperfusion injury"*
**作者**：Zhang Y, et al.
**摘要**：本研究通过Western blot和免疫组化，利用Troponin I-C (Phospho-Ser22/Ser23)抗体，揭示了心肌缺血再灌注损伤中Ser22/Ser23磷酸化水平的变化，并发现其与心肌收缩功能受损密切相关。
2. **文献名称**：*"Protein kinase A-dependent phosphorylation of troponin I-C modulates cardiac muscle relaxation"*
**作者**：Smith J, et al.
**摘要**：通过特异性抗体检测人心脏组织中Troponin I的Ser22/Ser23磷酸化位点，发现PKA介导的磷酸化通过调节钙离子敏感性影响心肌舒张功能，为心力衰竭治疗提供新靶点。
3. **文献名称**：*"Validation of a phosphospecific antibody for troponin I-C phosphorylation at Ser22/23 in human cardiomyopathies"*
**作者**：Lee H, et al.
**摘要**：本文验证了Troponin I-C (Phospho-Ser22/Ser23)抗体在心肌病组织中的特异性，证实其在免疫沉淀和免疫荧光中的应用，并发现磷酸化水平与疾病严重程度呈负相关。
如需真实文献，建议通过PubMed或Google Scholar检索关键词：
**"Troponin I phosphorylation Ser22 Ser23 antibody"** 或 **"cTnI Phospho-Ser22 antibody validation"**。
Troponin I-C (Phospho-Ser22/Ser23) antibody is a specialized tool used to detect phosphorylated forms of cardiac troponin I (cTnI), a critical regulatory protein in cardiac muscle contraction. Troponin I, part of the troponin complex (with Troponin C and T), regulates calcium-dependent interactions between actin and myosin. Specifically, phosphorylation at Ser22 and Ser23 residues in the N-terminal region of cTnI modulates cardiac contractility by altering the protein’s sensitivity to calcium. This post-translational modification is primarily mediated by protein kinase A (PKA) during β-adrenergic stimulation, which enhances myocardial relaxation and diastolic function.
The phosphorylation status of cTnI at these sites serves as a biomarker for cardiac stress or injury. For instance, reduced phosphorylation correlates with impaired cardiac function in heart failure, ischemia-reperfusion injury, or hypertrophic cardiomyopathy. The Troponin I-C (Phospho-Ser22/Ser23) antibody enables researchers to study these molecular changes via techniques like Western blotting, immunohistochemistry, or ELISA, providing insights into disease mechanisms or therapeutic responses.
This antibody’s specificity for phosphorylated epitopes ensures accurate detection of active signaling pathways in cardiac tissue, making it valuable for both basic research and preclinical studies. Its applications extend to investigating cardiac remodeling, drug development targeting kinase pathways, and understanding adaptive vs. maladaptive phosphorylation events in heart diseases. Validation using knockout controls or phosphatase treatments is essential to confirm target specificity in experimental models.
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