| 货号 | AF3627-SP |
| 别名 | Glycoprotein 6; glycoprotein VI (platelet); GP6; GPIV; GPVIplatelet collagen receptor; MGC138168; platelet glycoprotein VI | 全称 | Glycoprotein VI [Platelet] |
| 反应种属 | Human |
| 应用 | Western Blot(0.1 µg/mL) |
| 目标/特异性 | Detects human GPVI in direct ELISAs and Western blots. |
| 使用方法 | Western Blot: 0.1 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 | 51206 (Human); 243816 (Mouse) |
| 纯化方式 | Antigen Affinity-purified |
| 免疫原 | Mouse myeloma cell line NS0-derived recombinant human GPVI (R&D Systems, Catalog # 3627-GP) Gln21-Lys267 Accession # Q9HCN6 |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 背景 | Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation (1, 2). GPVI is also a secondary receptor required for platelet spreading on laminin (3). Human GPVI contains a 20 amino acid (aa) signal sequence, a 247 aa extracellular domain (ECD) that has two C-type Ig-like domains followed by a mucin-like, presumably O-glycosylated Ser-Thr-rich region, a 21 aa transmembrane (TM) domain and a 51 aa cytoplasmic tail that contains calmodulin-binding and SH3 domains. Human GPVI ECD shows 69%, 65% and 70% aa identity with mouse, bovine and canine GPVI ECD, respectively. Two splice variants exist; one is 17 aa shorter in the ECD, while the other diverges at aa 260, creating an inactive monomeric and presumably secreted 681 aa protein (3). GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid) (2). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence (2). Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding (5, 6). Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques (7). GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2beta1 which binds collagen more tightly (8). GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2beta1 is able to minimally initiate collagen binding (8). Normal human GPVI concentration can vary widely and affect maximum thrombin generation (9). Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI (10). |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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