阿拉丁重组蛋白

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为什么选择此级别

ActiBioPure™,EnzymoPure™,天然,生物活性,高性能级，适用于对基线干扰要求严格的色谱和分析工作流程。

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储存与运输

-20°C储存,避免反复冻融。超低温运输。请查阅批次 COA 获取详细规格。

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质量文档

SDS、COA、产品数据表及规格说明书均可下载。可通过批号查询获取批次 COA。

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文献证明

在色谱分析、有机合成和交叉偶联反应领域已被 34 篇同行评审文献引用。

概述

凝血酶是止血过程中的最终凝血蛋白酶，可同时促进促凝血和抗凝血作用。选择性裂解纤维蛋白原中 Arg-Gly 键形成纤维蛋白和纤维蛋白肽 A 和 B 的丝氨酸蛋白酶。

冻干粉末，含有蔗糖、氯化钠和Tris。

应用：

凝血酶被用于重组融合蛋白的位点特异性切割，这些重组融合蛋白具有可接近的凝血酶识别位点以除去亲和标签。凝血酶已应用于一项研究，以评估用于小尺寸血小板微粒的流式细胞术的创新方法。

分析说明：

活性以NIH单位表示，它是通过与NIH凝血酶参考标准品直接对比而获得的.

NIH测定程序根据Biggs改进方法，使用0.2ml稀释血浆（与生理盐水1:1）作为底物以及0.1ml凝血酶样本（在1%缓冲白蛋白溶液中稳定）。仅在15-25 秒的凝血时间内测定凝血酶浓度。

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.

Lyophilized powder containing sucrose, sodium chloride and Tris.

Application:

Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. Thrombin has been used in a study to assess an innovative flow cytometric approach for small-size platelet microparticles.

Analysis Note

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard.

The NIH assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations.

规格

产品名称

凝血酶

规格或纯度

生物活性,ActiBioPure™,天然,高性能,EnzymoPure™,来源于人血浆; 400-1000 NIH U/mg protein

生化机理

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces. Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells. Miscellaneous: It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting. Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa. The cleavage after Arg-198, observed in vitro, does not occur in plasma. Catalytic activity: Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. Activity regulation: Activity is promoted in the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate. Inhibited by SERPINA5. Post-translational: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg-363, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-314, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-363, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-363, but has a smaller effect on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells.

生物活性

400-1000 NIH U/mg protein

种属

人(Human)

Accession #

P00734

来源

天然

CAS编号和信息

9002-04-4

酶学委员会编号

3.4.21.5

分子类型

酶

储存与运输

物理形态

冻干(Lyophilized)

储存缓冲液

Lyophilized from Sucrose, Sodium chloride, Tris.

浓度

来源于人血浆; 400-1000 NIH U/mg protein

复溶

Reconstitute in 1% buffered Albumin solution.

储存条件

-20°C储存,避免反复冻融

运输条件

超低温运输

稳定性与储存

长期储存-20℃；复溶后建议分装，避免反复冻融。

单位定义

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard. The NIH assay procedure uses 0.2 mL plasma diluted 1:1 with saline as substrate and 0.1 mL of Thrombin sample diluted in 1% buffered Albumin solution. B

技术文档

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全面的危险、操作、储存及法规合规文件。

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高级数据

产品属性

Nacres	NA.54

质检证书（CoA,COO,BSE/TSE 和分析图谱)

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找到3个结果

批号(Lot Number)	证书类型	货号
ZJ26F0737596	分析证书	T754968
ZJ26F0535772	分析证书	T754968
ZJ26F0232245	分析证书	T754968

技术文档和文章

凝血酶的结构功能、制备技术及应用研究进展

目录：技术文章

探索主题:

丝氨酸蛋白酶质量控制凝血酶重组制备局部止血

Structural–Functional Characteristics, Production Technologies, and Application Progress of Thrombin

目录：技术文章

探索主题:

Serine protease Quality control Thrombin Recombinant production Topical hemostasis

止血、纤溶与血管稳态中的蛋白酶功能体系及调控逻辑

目录：技术文章

探索主题:

蛋白酶凝血酶内皮功能止血纤溶纤溶酶活化蛋白C ADAMTS13 血管稳态血栓形成

Proteinase Functional Systems and Regulatory Logic in Hemostasis, Fibrinolysis, and Vascular Homeostasis

目录：技术文章

探索主题:

Thrombin proteases endothelial function ADAMTS13 Hemostasis Fibrinolysis Plasmin Activated Protein C Vascular Homeostasis Thrombosis

凝血与抗凝蛋白网络在心血管疾病中的动态重构与研究体系

目录：技术文章

探索主题:

心血管疾病凝血酶纤溶凝血抗凝组织因子蛋白C 抗凝血酶组织因子途径抑制物血管性血友病因子

Dynamic Remodeling of the Coagulation-Anticoagulation Protein Network in Cardiovascular Diseases and Its Research Framework

目录：技术文章

探索主题:

Cardiovascular diseases Thrombin Fibrinolysis Coagulation Anticoagulation Tissue Factor Protein C Antithrombin Tissue Factor Pathway Inhibitor Von Willebrand Factor

医用水凝胶研发中的关键判断：从聚合物来源、交联方式到灭菌安排、放大可行性与质量控制

目录：技术文章

探索主题:

医用水凝胶

Key Judgments in Medical Hydrogel R&D: From Polymer Source and Crosslinking Strategy to Sterilization Planning, Scale-Up Feasibility, and Quality Control

目录：技术文章

探索主题:

Medical hydrogels

纤溶活性蛋白酶研究方法与应用：血栓溶解、纤维蛋白降解和抗凝评价

目录：技术文章

探索主题:

PT 凝血酶 APTT 纤溶酶纤溶活性蛋白酶血栓溶解纤维蛋白降解纤溶酶原尿激酶链激酶蚓激酶纳豆激酶纤维蛋白平板法凝块溶解实验纤维蛋白原降解抗凝活性 TT 凝血因子Xa

Research Methods and Applications of Fibrinolytic Proteases: Thrombolysis, Fibrin Degradation, and Anticoagulant Evaluation

目录：技术文章

探索主题:

PT Thrombin APTT Plasmin TT Fibrinolytic protease Thrombolysis Fibrin degradation Plasminogen Urokinase Streptokinase Lumbrokinase Nattokinase Fibrin plate method Clot lysis assay Fibrinogen degradation Anticoagulant activity Coagulation factor Xa

内肽酶与外肽酶的功能差异及其在疾病机制研究中的应用

目录：技术文章

探索主题:

蛋白质降解 Endopeptidase 氨基肽酶外肽酶 exopeptidase 内肽酶肽段加工羧肽酶二肽基肽酶

Functional Differences Between Endopeptidases and Exopeptidases and Their Applications in Disease Mechanism Research

目录：技术文章

探索主题:

Protein degradation Endopeptidase aminopeptidase exopeptidase Peptide Processing carboxypeptidase dipeptidyl peptidase

融合蛋白标签切除：常用蛋白酶的催化机制、识别特异性与选择策略

目录：技术文章

探索主题:

凝血酶融合蛋白标签切除 TEV蛋白酶 HRV 3C蛋白酶肠激酶 Factor Xa SUMO蛋白酶识别序列重组蛋白纯化

Fusion-Protein Tag Removal: Catalytic Mechanisms, Recognition Specificity, and Selection Strategies of Common Proteases

目录：技术文章

探索主题:

Thrombin Factor Xa fusion protein tag removal TEV protease HRV 3C protease enterokinase SUMO protease recognition sequence recombinant protein purification

纤连蛋白的结构与功能：细胞黏附、皮肤创伤修复与外用应用

目录：技术文章

探索主题:

纤连蛋白 FN

Structure and Functions of Fibronectin: Cell Adhesion, Cutaneous Wound Repair, and Topical Applications

目录：技术文章

探索主题:

fibronectin FN

丝氨酸内切蛋白酶的催化机制、分类特征与实验应用

目录：技术文章

探索主题:

胰蛋白酶丝氨酸蛋白酶凝血酶催化三联体蛋白水解丝氨酸内切蛋白酶 EC 3.4.21 枯草杆菌蛋白酶

Catalytic Mechanisms, Classification Characteristics, and Experimental Applications of Serine Endopeptidases

目录：技术文章

探索主题:

Trypsin Thrombin Subtilisin catalytic triad proteolysis EC 3.4.21 serine endopeptidases serine proteases

此产品的引用文献

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引用文献

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