추천 제품
양식
lyophilized powder
Quality Level
특이 활성도
600-2,000 NIH units/mg protein (biuret)
분자량
heavy chain ~33 kDa
light chain ~5 kDa
UniProt 수납 번호
응용 분야
diagnostic assay manufacturing
저장 온도
−20°C
유전자 정보
cow ... F2(280685)
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관련 카테고리
일반 설명
Thrombin is a sodium-activated type II enzyme. It contains two anion binding exosites, ABE-I and ABE-II. The predominant form of thrombin in vivo is the zymogen prothrombin (factor II), which is produced in the liver. Bovine a-thrombin consists of a light chain (A chain) and a heavy chain (B chain). These two chains are joined by one disulfide bond. The B chain of a-thrombin includes a carbohydrate portion.
애플리케이션
Thrombin from bovine plasma has been used to study its effect on the perinatal rat subventricular zone cells and oligodendrocyte precursor cell proliferation, differentiation, and migration in culture. It has also been used in fibrin degradation assay to measure nattokinase activity.
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 global haemostasis and point of care testing.
생화학적/생리학적 작용
Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
Thrombin is a proteolytic enzyme critical in the blood clotting process and activates clotting factors V, VIII, XI, and XII. Thrombin promotes platelet aggregation. Therefore, thrombin is the final coagulation protease in hemostasis, promoting both procoagulant and anticoagulant effects. It is used to treat bleeding from capillaries and small venules.
단위 정의
Activity is expressed in NIH units obtained by direct comparison to a NIH thrombin reference standard.
물리적 형태
Lyophilized from saline sodium citrate buffer, pH 6.5
분석 메모
Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard, Lot K.
The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL 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.
기타 정보
View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.
기질
저해제
제품 번호
설명
가격
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
표적 기관
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
Y Dargaud et al.
Haemophilia : the official journal of the World Federation of Hemophilia, 18 Suppl 4, 81-88 (2012-06-29)
The evaluation of the coagulation profile has used so far either clotting-based or chromogenic assays with different endpoints. Clotting-based techniques are the most used worldwide, and they certainly are useful for diagnosis of clotting factor deficiencies. However, the information provided
Thrombin as an Agent
xPharm: The Comprehensive Pharmacology Reference null
Thrombin as a Target
xPharm: The Comprehensive Pharmacology Reference null
Ting-Yuan Tu et al.
Frontiers in bioengineering and biotechnology, 10, 877480-877480 (2022-05-20)
Blood vessels are ubiquitous in the human body and play essential roles not only in the delivery of vital oxygen and nutrients but also in many disease implications and drug transportation. Although fabricating in vitro blood vessels has been greatly
Shiyang Cao et al.
Nature communications, 13(1), 4526-4526 (2022-08-05)
Plague has caused three worldwide pandemics in history, including the Black Death in medieval ages. Yersinia pestis, the etiological agent of plague, has evolved a powerful arsenal to disrupt host immune defenses during evolution from enteropathogenic Y. pseudotuberculosis. Here, we
문서
Thrombin Factor IIa is an endolytic serine protease that selectively cleaves the Arg--Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.
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