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SRP6556

Sigma-Aldrich

Thrombin Active (High Activity) from bovine plasma

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

Synonym(s):

Activated Factor IIa

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

product name

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

biological source

bovine plasma

Assay

≥98% (SDS-PAGE)

form

lyophilized

potency

>1500 units/mg

mol wt

37 kDa

packaging

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

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

bovine ... F2(280685)

General description

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

Biochem/physiol Actions

Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. 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. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. 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. 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. It is also involved in the activation of protein C which is needed for the inactivation of many procoagulant enzymes.

Physical form

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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)
Exogenous thrombin delivery promotes collateral capillary arterialization and tissue reperfusion in the murine spinotrapezius muscle ischemia model.
Bruce AC and Peirce SM
Microcirculation (New York, N.Y. : 1994), 19, 143-154 (2012)
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)

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