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T9326

Sigma-Aldrich

Thrombin human

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

Sinónimos:

Factor IIa

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About This Item

Comisión internacional de enzimas:
3.4.21.5 (BRENDA, IUBMB)
MDL number:
MFCD00082072
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in HEK 293 cells

Quality Level

200

product line

BioUltra

assay

≥95% (SDS-PAGE)

form

aqueous solution

specific activity

≥2,000 units/mg protein

mol wt

37.4 kDa

UniProt accession no.

P00734

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... F2(2147)

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General description

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.

Unit Definition

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

Physical form

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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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
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
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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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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