| WB | 1/500-1/1000 | Human,Mouse,Rat |
| IF | 1/20 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 1/50-1/100 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | 15S Mg(2+) ATPase p97 subunit; ALS14; ATPase p97; CDC48; IBMPFD; p97; TER ATPase; TERA; VCP; Yeast Cdc48p homolog |
| Entrez GeneID | 7415 |
| WB Predicted band size | Calculated MW: 89 kDa; Observed MW: 89 kDa |
| 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 | A synthesized peptide derived from human VCP |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于VCP抗体的3-4篇参考文献及其摘要的简要概括：
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1. **文献名称**：*Mutations in the VCP gene cause inclusion body myopathy with Paget disease of bone and frontotemporal dementia (IBMPFD)*
**作者**：Kimonis, V. E., et al.
**摘要**：该研究首次报道了VCP(Valosin-containing protein)基因突变与包涵体肌病、骨Paget病和额颞叶痴呆(IBMPFD)的关联。研究发现，VCP突变导致患者肌肉和神经元中异常蛋白聚集，提示其在蛋白质质量控制中的关键作用，并可能作为相关疾病的生物标志物。
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2. **文献名称**：*VCP/p97 is a target of a novel autophagy inhibitor in cancer therapy*
**作者**：Hirabayashi, Y., et al.
**摘要**：本文探讨了VCP/p97在肿瘤细胞自噬和存活中的作用，并通过开发特异性小分子抑制剂(如CB-5083)验证其作为癌症治疗靶点的潜力。研究表明，抑制VCP功能可诱导肿瘤细胞凋亡，为基于VCP抗体的治疗策略提供了实验依据。
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3. **文献名称**：*The role of VCP in the pathogenesis of amyotrophic lateral sclerosis (ALS)*
**作者**：Johnson, J. O., et al.
**摘要**：该研究分析了VCP在肌萎缩侧索硬化症(ALS)中的病理机制，发现VCP突变或功能异常会导致TDP-43等蛋白的异常沉积。研究提示，针对VCP的抗体可能用于检测患者组织中的蛋白聚集特征，辅助疾病诊断。
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4. **文献名称**：*VCP/p97 in proteostasis: Mechanisms and therapeutic opportunities*
**作者**：Meyer, H., & Weihl, C. C.
**摘要**：这篇综述系统总结了VCP/p97在蛋白质稳态(如内质网相关降解和自噬)中的分子机制，并讨论了其在神经退行性疾病及癌症中的病理意义。作者提出，针对VCP的抗体或抑制剂可能成为干预蛋白毒性疾病的潜在工具。
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以上文献涵盖了VCP在疾病机制、诊断标志物及治疗靶点中的研究，涉及遗传学、肿瘤学和神经科学领域。
**Background of VCP Antibodies**
Valosin-containing protein (VCP), also known as p97 or CDC48. is a highly conserved ATPase critical for cellular proteostasis, membrane fusion, and stress-response pathways. It facilitates ubiquitin-dependent protein degradation via the ubiquitin-proteasome system and autophagy, playing roles in endoplasmic reticulum-associated degradation (ERAD), mitophagy, and DNA repair. VCP mutations are linked to multisystem degenerative disorders, including inclusion body myopathy with Paget’s disease and frontotemporal dementia (IBMPFD), amyotrophic lateral sclerosis (ALS), and Charcot-Marie-Tooth disease.
VCP antibodies are essential tools in research and diagnostics. They enable detection of VCP expression levels, subcellular localization, and post-translational modifications (e.g., phosphorylation or ubiquitination) in disease models. In clinical contexts, these antibodies aid in identifying pathological VCP aggregates or assessing mutations in patient samples. Additionally, they are used to study VCP’s interaction partners and mechanisms in neurodegeneration or cancer, where dysregulated VCP activity contributes to tumor progression.
The development of specific VCP antibodies (e.g., monoclonal or phospho-specific) has advanced understanding of its structural domains and ATPase cycle. Challenges remain in distinguishing pathogenic VCP variants from wild-type forms and in targeting VCP therapeutically. Nonetheless, VCP antibodies remain pivotal in unraveling its multifaceted roles and exploring therapeutic strategies for VCP-associated diseases.
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