WB | 咨询技术 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 咨询技术 | Human,Mouse,Rat |
ICC | 技术咨询 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 咨询技术 | Human,Mouse,Rat |
Aliases | CMH7, RCM1, cTnI, CMD2A, TNNC1 |
Entrez GeneID | 7137; |
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 | Human,Mouse,Rat |
Immunogen | Peptide sequence around phosphorylation site of Threonine 142 (R-P-T(p)-L-R) derived from Human TNNI3. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇关于TNNI3 (Phospho-Thr142)抗体的参考文献示例(内容为模拟生成,仅供参考):
1. **标题**:*"Phosphorylation of cardiac troponin I at Thr142 regulates myocardial function in ischemia-reperfusion injury"*
**作者**:Zhang L, et al.
**摘要**:该研究利用TNNI3 (Phospho-Thr142)特异性抗体,发现心肌缺血再灌注损伤中Thr142位点的磷酸化水平显著升高,并通过体外实验证实其通过调节钙离子敏感性加剧心肌细胞凋亡。
2. **标题**:*"Development and validation of a phosphospecific antibody for detecting TNNI3 phosphorylation at Thr142 in human cardiomyopathy"*
**作者**:Wang Y, et al.
**摘要**:研究团队开发并验证了一种高特异性TNNI3 (Phospho-Thr142)多克隆抗体,通过质谱和免疫印迹确认其特异性,并应用于扩张型心肌病患者组织样本,发现该位点磷酸化与疾病严重程度相关。
3. **标题**:*"Akt-mediated phosphorylation of cardiac troponin I at Thr142 contributes to pathological cardiac hypertrophy"*
**作者**:Chen H, et al.
**摘要**:利用Phospho-Thr142抗体揭示Akt激酶通过磷酸化TNNI3的Thr142位点,促进心肌肥厚信号通路,为靶向该位点的治疗策略提供了实验依据。
4. **标题**:*"Site-specific phosphorylation of troponin I by protein kinase C regulates cardiac contractility"*
**作者**:Johnson KR, et al.
**摘要**:研究通过Phospho-Thr142抗体发现PKCα对TNNI3的Thr142磷酸化负向调控心肌收缩力,为心力衰竭的分子机制提供了新见解。
(注:以上文献为示例性内容,实际引用需查询真实数据库如PubMed或Google Scholar。)
TNNI3 (Phospho-Thr142) antibody is a specialized immunological tool designed to detect the phosphorylated form of cardiac troponin I (cTnI) at threonine residue 142. TNNI3. encoded by the TNNI3 gene, is a key regulatory protein in cardiac muscle contraction. It functions as part of the troponin complex, modulating calcium-dependent interactions between actin and myosin during the cardiac cycle. Phosphorylation at specific residues, including Thr142. plays a critical role in fine-tuning cardiac muscle function by altering the sensitivity of myofilaments to calcium.
The Thr142 phosphorylation site is particularly associated with protein kinase C (PKC)-mediated signaling pathways, which are implicated in cardiac stress responses, hypertrophy, and heart failure. Aberrant phosphorylation at this site has been linked to impaired contractility and pathological cardiac remodeling. The TNNI3 (Phospho-Thr142) antibody enables researchers to investigate these mechanisms by selectively identifying the phosphorylated state of TNNI3 in experimental models, such as heart tissue samples or cultured cardiomyocytes.
This antibody is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to study cardiac pathophysiology, drug effects on phosphorylation dynamics, and biomarker discovery for heart diseases. Its specificity for the phosphorylated epitope makes it valuable for distinguishing activated signaling states in both basic research and clinical investigations.
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