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T9326

Sigma-Aldrich

Thrombin human

BioUltra, recombinant, expressed in HEK 293 cells, aqueous solution, ≥95% (SDS-PAGE)

Synonyme(s) :

Factor IIa

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About This Item

Numéro de classification (Commission des enzymes):
3.4.21.5 (BRENDA, IUBMB)
Numéro MDL:
MFCD00082072
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in HEK 293 cells

Niveau de qualité

200

Gamme de produits

BioUltra

Pureté

≥95% (SDS-PAGE)

Forme

aqueous solution

Activité spécifique

≥2,000 units/mg protein

Poids mol.

37.4 kDa

Numéro d'accès UniProt

P00734

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... F2(2147)

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Catégories apparentées

Description générale

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.

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 in vitro hemostatic properties of French lyophilized plasma.

Définition de l'unité

Activity is expressed in NIH units obtained by direct comparison to a NIH thrombin reference standard.

Forme physique

supplied as a solution in 20 mM MES, pH 6.0, 500 mM choline chloride

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Christophe Martinaud et al.
Anesthesiology, 117(2), 339-346 (2012-06-29)
French lyophilized plasma (FLyP) is used routinely by the French Armed Forces in war settings. The authors compared concentrations of coagulation proteins and global in vitro hemostatic properties in FLyP and in the same plasma before lyophilization to assess the
Katerina Zakharova et al.
International journal of molecular sciences, 22(14) (2021-07-25)
Redβ is a 261 amino acid protein from bacteriophage λ that promotes a single-strand annealing (SSA) reaction for repair of double-stranded DNA (dsDNA) breaks. While there is currently no high-resolution structure available for Redβ, models of its DNA binding domain
Ute Metzger et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(34), 14309-14314 (2009-08-27)
Ergot alkaloids are toxins and important pharmaceuticals that are produced biotechnologically on an industrial scale. The first committed step of ergot alkaloid biosynthesis is catalyzed by dimethylallyl tryptophan synthase (DMATS; EC 2.5.1.34). Orthologs of DMATS are found in many fungal
Dmitriy Krepkiy et al.
Nature, 462(7272), 473-479 (2009-11-27)
Despite the growing number of atomic-resolution membrane protein structures, direct structural information about proteins in their native membrane environment is scarce. This problem is particularly relevant in the case of the highly charged S1-S4 voltage-sensing domains responsible for nerve impulses
Diane Moujalled et al.
Cell death & disease, 12(1), 133-133 (2021-01-30)
Necroptosis is a pro-inflammatory cell death program executed by the terminal effector, mixed lineage kinase domain-like (MLKL). Previous studies suggested a role for the necroptotic machinery in platelets, where loss of MLKL or its upstream regulator, RIPK3 kinase, impacted thrombosis
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Articles

Thrombin Factor IIa

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.

Thrombin Factor IIa

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.

Thrombin Factor IIa

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.

Thrombin Factor IIa

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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