SRP6556
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.
Preparation Note
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
Regulatory Information
低风险生物材料
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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)
Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.
Sabo TM and Maurer MC
Biochemistry, 48, 7110-7122 (2009)
A dual thrombin receptor system for platelet activation.
Kahn ML, et al.
Nature, 394, 690-694 (1998)
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)
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)
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