货号 | AF4245-SP |
别名 | A disintegrin and metalloproteinase with thrombospondin motifs 13; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondintype 1 motif, 13; ADAM metallopeptidase with thrombospondin type 1 motif, 13; ADAM-TS13; ADAMTS-13; DKFZp434C2322; EC 3.4.24.14; EC 3.4.24.82; EC 3.4.24.87; FLJ42993; MGC118899; MGC118900; TTP; TTPADAM-TS 13; vWF-cleaving protease; vWF-CP; vWF-CPC9orf8; VWFCPvon Willebrand factor-cleaving protease | 全称 | A Disintegrin-like and Metalloproteinase Domain with Thrombospondin Motifs 13 |
反应种属 | Human |
应用 | Western Blot(0.1 µg/mL) Immunoprecipitation(25 µg/mL) |
目标/特异性 | Detects human ADAMTS13 in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 1% cross‑reactivity with recombinant human (rh) ADAMTS1, rhADAMTSL-1.2, rhADAMTS4, and rhADAMTS5 is observed. |
使用方法 | Western Blot: 0.1 µg/mL Immunoprecipitation: 25 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 | 11093 (Human); 279028 (Mouse); 362091 (Rat) |
纯化方式 | Antigen Affinity-purified |
免疫原 | Chinese hamster ovary cell line CHO-derived recombinant human ADAMTS13 Gln34-Trp688 Accession # Q76LX8 |
生物活性 | Human |
标记 | Unconjugated |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | ADAMTS13 (A disintegrin and metalloprotease with TSP motifs 13) is a 140-230 kDa, secreted glycoprotein member of the ADAMTS family of proteases. ADAMTS13 is produced by the liver and circulates in plasma where it cleaves and reduces the activity of von Willebrand factor. ProADAMTS13 is 1398 amino acids (aa) in length. It contains a 45 aa prodomain (aa 30-74), one peptidase domain (aa 80-286) and one disintegrin (aa 287-383) domain, multiple TSP regions and two CUB domains. The prodomain does not affect activity, while the TSP and CUB domains appear to be necessary for activity. One truncated form exists that shows truncation after Gln448. Over aa 34-688, human ADAMST13 shares 76% aa identity with mouse ADAMST13. |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
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