| 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 | 1/5000 | Human,Mouse,Rat |
| Aliases | VCP; Transitional endoplasmic reticulum ATPase; TER ATPase; 15S Mg(2+)-ATPase p97 subunit; Valosin-containing protein; VCP |
| Entrez GeneID | 7415; |
| WB Predicted band size | 85kDa |
| 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 | Synthesized peptide derived from human VCP around the phosphorylation site of S352. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是基于假设的示例参考文献，用于演示可能的格式和内容。实际文献需通过学术数据库核实：
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1. **文献名称**: "Phosphorylation of VCP at Ser352 regulates its interaction with UBXD7 during ER stress"
**作者**: Smith J, et al.
**摘要**: 研究揭示了VCP在Ser352位点的磷酸化在内质网应激中的关键作用。磷酸化增强了VCP与衔接蛋白UBXD7的结合，促进错误折叠蛋白的降解，提示其在未折叠蛋白反应(UPR)中的调控机制。
2. **文献名称**: "ATM-dependent phosphorylation of VCP/p97 modulates DNA repair pathways"
**作者**: Johnson L, et al.
**摘要**: 本文发现DNA损伤后，ATM激酶介导VCP Ser352磷酸化，增强其与DNA修复复合体的结合，促进损伤位点的染色质重塑，表明该修饰在基因组稳定性中的重要性。
3. **文献名称**: "Phospho-Ser352 VCP as a biomarker for chemotherapy resistance in colorectal cancer"
**作者**: Chen R, et al.
**摘要**: 通过分析癌症样本，发现VCP Ser352磷酸化水平升高与奥沙利铂耐药性相关，机制涉及自噬通路的异常激活，提示其作为治疗靶点的潜力。
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**注意**：以上文献为示例，实际引用需查询PubMed、Web of Science等平台，建议使用关键词“VCP phosphorylation Ser352”或抗体货号(如Abcam或CST的产品说明书引用文献)。
The VCP (Phospho-Ser352) antibody is designed to detect valosin-containing protein (VCP), also known as p97 or CDC48. specifically when phosphorylated at serine residue 352. VCP is a member of the AAA+ (ATPases Associated with diverse cellular Activities) ATPase family, involved in critical cellular processes such as ubiquitin-proteasome degradation, endoplasmic reticulum-associated degradation (ERAD), autophagy, and DNA repair. Phosphorylation at Ser352 is a post-translational modification that regulates VCP's ATPase activity, substrate binding, or interactions with cofactors, thereby modulating its role in protein homeostasis and stress response. This site lies within the N-terminal domain, which is critical for binding adaptor proteins and coordinating substrate processing.
The antibody is widely used in research to study VCP's regulatory mechanisms in diseases linked to its dysfunction, including inclusion body myopathy with Paget’s disease and frontotemporal dementia (IBMPFD), amyotrophic lateral sclerosis (ALS), and cancers. Detection of phosphorylated VCP helps elucidate its activation state under cellular stress, DNA damage, or pathological conditions. Researchers employ this tool in techniques like Western blotting, immunofluorescence, and immunohistochemistry to explore VCP's phosphorylation dynamics in cell lines, tissue samples, or disease models. Its specificity for the Ser352-phosphorylated form makes it valuable for dissecting signaling pathways involving VCP and evaluating therapeutic interventions targeting its activity.
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