| 货号 | AF5820-SP |
| 别名 | hVAP-33; MGC3745,33 kDa VAMP-associated protein; VAMP (vesicle-associated membrane protein)-associated protein A, 33kDa; VAMP-A; VAP-33; VAP33VAMP (vesicle-associated membrane protein)-associated protein A (33kD); VAP-AVAMP-associated protein A; vesicle-associated membrane protein-associated protein A | 全称 | VAMP [Vesicle-associated Membrane Protein]-associated Protein A |
| 反应种属 | Human |
| 应用 | Western Blot(1 µg/mL) |
| 目标/特异性 | Detects human VAP-A in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross-reactivity with recombinant human VAP-B and recombinant rat VAP-B is observed. |
| 使用方法 | Western Blot: 1 µg/mL |
| 来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 9218 (Human); 30960 (Mouse); 58857 (Rat) |
| 纯化方式 | Antigen Affinity-purified |
| 免疫原 | E. coli-derived recombinant human VAP-A Ala2-Met132 Accession # Q9P0L0 |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 背景 | Vesicle-associated membrane protein (VAMP)-associated protein A (VAP-A; also VAMP-A and VAP-33) is a 33 kDa, ubiquitously expressed, type IV transmembrane protein belonging to the VAP family of proteins. It is found in plasma and ER membranes as well as in intracellular vesicles as a homodimer and a heterodimer with VAP-B. Human VAP-A is synthesized as a 249 amino acid (aa) precursor that contains a 227 aa cytoplasmic domain and a 21 aa transmembrane region. The cytoplasmic domain contains a mobile sperm protein (MSP) domain (aa 14-131) and a coiled-coil region (aa 169-205). Human VAP-A is 97% aa identical to mouse and rat VAP-A. VAP-A and VAP-B recruit FFAT (two phenylalanines in an acidic tract)-motif-containing proteins to the cytosolic surface of ER membranes through a conserved region within their MSP domain, and they have been implicated in regulation of membrane transport, phospholipid biosynthesis, and the unfolded protein response. Their role in maintaining the identities of intracellular organelles has not been demonstrated, but their ability to interact with lipid-transfer/binding proteins (LT/BPs) may affect the lipid composition of certain cellular membranes. One study shows that VAPs play a critical role in maintaining the structural and functional properties of the Golgi complex. Researchers found that knockdown of VAP reduces the levels of phosphatidylinositol-4-phosphate (PI4P), diacylglycerol (DAG), and sphingomyelin (SM) in Golgi membranes and exports pleiotropic effects in Golgi-mediated transport. The effects of VAPs are mediated by their interacting FFAT-motif-containing proteins Nir2, OSBP, and CERT. VAPs provide a scaffold for these LT/BPs at the ER-Golgi membrane contact sites, thereby affecting the lipid composition of the Golgi membranes and consequently their structural and functional identities. Most recently, researchers found that VAP-A associates and co-localizes with protrudin, a protein that promotes neurite formation, and found that it was an important regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth. |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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Detection of Human VAP-A by Western Blot. Western blot shows lysates of HEK293 human embryonic kidney cell line and human heart tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti- Human VAP-A Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5820) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for VAP-A at approximately XXX kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8. |
