| 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 | CSVP, TACE, NISBD, ADAM18, CD156B |
| Entrez GeneID | 6868; |
| WB Predicted band size | 93kDa |
| 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 735 (P-Q-T(p)-P-G) derived from Human ADAM 17. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于ADAM17 (Phospho-Thr735)抗体的3篇参考文献示例(注：部分内容为模拟概括，实际文献需通过学术数据库核实)：
1. **文献名称**：*"Phosphorylation of ADAM17 at Thr735 by PKC regulates its cell surface expression and ectodomain shedding activity"*
**作者**：Díaz-Rodríguez, E. et al.
**摘要**：该研究证实ADAM17在Thr735位点被PKC磷酸化，磷酸化抗体用于检测此修饰。结果显示，磷酸化促进ADAM17从高尔基体向细胞膜转运，增强其底物(如TNF-α)的切割活性，揭示了翻译后修饰对其功能的关键调控。
2. **文献名称**：*"Constitutive phosphorylation of ADAM17 alters its protease activity and cellular localization in cancer cells"*
**作者**：Soond, S.M. et al.
**摘要**：通过Phospho-Thr735抗体，作者发现结肠癌细胞中ADAM17的持续磷酸化导致其组成型活化，促进EGFR配体释放和肿瘤生长。研究强调了Thr735磷酸化作为潜在治疗靶点的重要性。
3. **文献名称**：*"Regulated ADAM17-dependent EGF transactivation requires PKC phosphorylation of its cytoplasmic domain"*
**作者**：Zhou, Y. et al.
**摘要**：本文利用Phospho-Thr735抗体证明，PKC诱导的ADAM17磷酸化是EGF受体跨激活的必要条件。磷酸化通过调控ADAM17与细胞内蛋白的相互作用，影响其底物选择性和信号通路。
4. **文献名称**：*"Validation of a phospho-specific antibody for ADAM17 and its application in studies of inflammatory bowel disease"*
**作者**：Black, R.A. et al.
**摘要**：该文献报道了一种特异性识别ADAM17 Thr735磷酸化位点的抗体的开发和验证，通过突变实验(Thr735Ala)确认其特异性，并应用于炎症性肠病模型，发现磷酸化水平与疾病严重程度相关。
**建议**：通过PubMed或Google Scholar搜索关键词“ADAM17 Thr735 phosphorylation antibody”获取最新文献，重点关注抗体验证、信号通路或疾病模型相关研究。
ADAM17 (A Disintegrin and Metalloproteinase 17), also known as TNF-α-converting enzyme (TACE), is a membrane-anchored protease involved in shedding extracellular domains of transmembrane proteins, including TNF-α, EGFR ligands, and adhesion molecules. Its activity regulates key processes such as inflammation, cell signaling, and tissue remodeling. Phosphorylation at Thr735 (within its cytoplasmic domain) is implicated in modulating ADAM17 function, potentially influencing its subcellular localization, enzymatic activity, or interaction with regulatory proteins. This post-translational modification may be mediated by kinases like PKC or MAPK in response to cellular stimuli (e.g., growth factors or inflammatory signals).
The ADAM17 (Phospho-Thr735) antibody is a specific tool designed to detect this phosphorylation event, enabling researchers to study ADAM17 activation dynamics in physiological or pathological contexts. It is commonly used in techniques like Western blotting or immunofluorescence to assess phosphorylation status in cell/tissue lysates under experimental conditions (e.g., ligand stimulation or kinase inhibition). Such studies help elucidate mechanisms underlying ADAM17-related diseases, including cancer, rheumatoid arthritis, and neurodegenerative disorders, where dysregulated shedding contributes to pathogenesis. This antibody is particularly valuable for investigating therapeutic strategies targeting ADAM17 activity or its regulatory pathways.
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