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SRP6557

Sigma-Aldrich

Thrombin Active from human plasma

≥95% (SDS-PAGE)

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Synonym(s):
Activated Factor IIa
NACRES:
NA.32

biological source

human

Assay

≥95% (SDS-PAGE)

form

lyophilized

potency

>3000 units/mg

mol wt

37 kDa

packaging

pkg of 1000 units
pkg of 250 units

UniProt accession no.

P00734

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... F2(2147)

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This Item
T9326SRP655610602400001
Sigma-Aldrich

Sigma-Aldrich

SRP6557

Thrombin Active from human plasma

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

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T9326

Thrombin human

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SRP6556

Thrombin Active (High Activity) from bovine plasma

Thrombin from human plasma

Roche

10602400001

Thrombin

assay

≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

-

form

lyophilized

form

aqueous solution

form

lyophilized

form

lyophilized

potency

>3000 units/mg

potency

-

potency

>1500 units/mg

potency

-

mol wt

37 kDa

mol wt

37.4 kDa

mol wt

37 kDa

mol wt

Mr ~33.6 kDa

packaging

pkg of 1000 units, pkg of 250 units

packaging

-

packaging

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

packaging

pkg of 20 U

General description

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. It is primarily associated with blood clotting.

Biochem/physiol Actions

Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. It also induces inflammation. 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.

Physical form

Lyophilized from a buffer composed of 20 mM Bis-Tris, 150 mM NaCl and 0.1% PEG 8000, pH 6.5.

Reconstitution

A working stock solution can be prepared by adding 1 mL buffered saline, pH 7.4 (ex. 25 mM HEPES, 150 mM NaCl, 0.1% PEG 8000, pH 7.4). Further dilution should be made in buffer containing a suitable stabilizing agent such as 0.1%-1% Prionex, BSA, or PEG.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H319 - H334

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Certificates of Analysis (COA)

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Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug.
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