| 中文名稱 | 凝血酶(凝血因子II)重鏈抗體 |
| 別 名 | coagulation factor II; prothrombin; F2; Cf-2; Cf2; FII; F 2; coagulation factor II (thrombin); Coagulation factor II; Coagulation factor II precursor; F2; Factor II; Factor-II; Prothrombin; prothrombin B-chain; PT; serine protease; THRB; THRB_HUMAN; Thrombin; Thrombin heavy chain. |
研究領域 心血管 細胞生物 激酶和磷酸酶 合成與降解
抗體來源 Rabbit
克隆類型 Polyclonal
交叉反應 Human, Mouse, Rat, (predicted: Chicken, Pig, Cow, Horse, Rabbit, Fish, )
產(chǎn)品應用 ELISA=1:5000-10000 IHC-P=1:100-500 IHC-F=1:100-500 IF=1:100-500 （石蠟切片需做抗原修復）
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量 28/68kDa
細胞定位 細胞外基質(zhì) 分泌型蛋白
性 狀 Liquid
濃 度 1mg/ml
免 疫 原 KLH conjugated synthetic peptide derived from human Thrombin heavy chain:551-622/622
亞 型 IgG
純化方法 affinity purified by Protein A
儲 存 液 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存條件 Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
PubMed PubMed
產(chǎn)品介紹 Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.
Function:
Thrombin is an active enzyme in the earliest steps of the blood clot formation, generated from its circulating inactive precursor prothrombin. Thrombin is a glycoprotein formed by two peptides chains of 36 and 259 amino acids linked by disulfure bonds. Three important sites have been identified on the surface of the enzyme: The catalytic site that confers to the molecule its serine protease activity, the exosite one responsible for the binding of the substrate (fibrinogen or thrombin receptor) and
