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Principaux documents

SRP6556

Sigma-Aldrich

Thrombin Active (High Activity) from bovine plasma

≥98% (SDS-PAGE), recombinant, lyophilized

Synonyme(s) :

Activated Factor IIa

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Le tarif et la disponibilité ne sont pas disponibles actuellement.

Nom du produit

Thrombin Active (High Activity) from bovine plasma, ≥98% (SDS-PAGE)

Source biologique

bovine plasma

Essai

≥98% (SDS-PAGE)

Forme

lyophilized

Puissance

>1500 units/mg

Poids mol.

37 kDa

Conditionnement

pkg of 10,000 units
pkg of 100,000 units
pkg of 1000 units

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

bovine ... F2(280685)

Description générale

Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions.[1]

Actions biochimiques/physiologiques

Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands.[2] Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII.[1] Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet.[3] As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs.[4] After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity. Thrombin enzyme (Activated Factor IIa) also participates in inflammation and has mitogenic role on vascular cells.[5] It is also involved in the activation of protein C which is needed for the inactivation of many procoagulant enzymes.[6]

Forme physique

Sterile filtered and lyophilized with Mannitol and Sodium Chloride.

Reconstitution

Reconstitute in sterile water (100 U/mL) with 0.9% NaCl. It forms a clear solution.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.
Grutter MG, et al.
The Embo Journal, 9, 2361-2365 (1990)
Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.
Sabo TM and Maurer MC
Biochemistry, 48, 7110-7122 (2009)
The CUG codon is decoded in vivo as serine and not leucine in Candida albicans.
Santos MA and Tuite MF
Nucleic Acids Research, 23, 1481-1486 (1995)
A dual thrombin receptor system for platelet activation.
Kahn ML, et al.
Nature, 394, 690-694 (1998)
Effects of coagulation factor deficiency on plasma coagulation kinetics determined via thrombelastography: critical roles of fibrinogen and factors II, VII, X and XII.
Nielsen VG, et al.
Acta Anaesthesiologica Scandinavica, 49, 222-231 (2005)

Questions

  1. What is the molecular weight expressed in kilodaltons (kDa)?

    1 réponse
    1. The molecular weight is 37 kilodaltons (kDa).

      Utile ?

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