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Key Documents

Safety Information

T1063

Sigma-Aldrich

Thrombin from human plasma

lyophilized powder, ≥2800 NIH units/mg protein (E1%/280, 18.3)

Synonym(s):

Factor IIa

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250 μG
¥5,675.96

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Estimated to ship on2025年5月12日Details

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250 μG
¥5,675.96

About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

¥5,675.96


Estimated to ship on2025年5月12日Details

A recombinant, preservative-free antibody is available for your target. Try ZRB04338

Request a Bulk Order

form

lyophilized powder

Quality Level

specific activity

≥2800 NIH units/mg protein (E1%/280, 18.3)

mol wt

37.4 kDa

impurities

HIV, hepatitis B and hepatitis C, tested negative

UniProt accession no.

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

human ... F2(2147)

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Show Differences

1 of 4

This Item
T7009T6634T6884
specific activity

≥2800 NIH units/mg protein (E1%/280, 18.3)

specific activity

≥1,000 NIH units/mg protein (E1%/280, 18.3)

specific activity

600-2,000 NIH units/mg protein (biuret)

specific activity

≥2,000 NIH units/mg protein (E1%/280, 18.3)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

37.4 kDa

mol wt

37.4 kDa

mol wt

heavy chain ~33 kDa, light chain ~5 kDa

mol wt

37.4 kDa

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 evaluate the in vitro effect of low molecular weight heparin on thrombin generation in cirrhotic patients at different stages of liver disease. [1]

Biochem/physiol Actions

Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.

Unit Definition

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard

Physical form

Lyophilized from 0.02 M Bis/Tris buffer, pH 6.5, 0.15 M NaCl and 0.1% PEG-8000

Analysis Note

The NIH assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations.

Other Notes

View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

高风险级别生物产品--人源产品

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    Journal of leukocyte biology, 108(4), 1293-1306 (2020-07-15)
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    We propose a new sensor design that maximizes fluorescence contrast, inspired by whispering-gallery mode lasing (WGM). Aptamer-modified glass microspheres (cf. 1-38 μm) and thrombin are used as a model sensory cavity and target protein, respectively. Two types of microsphere are
    D David et al.
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    In haemophilia A, the functional defect at the molecular level of most factor VIII (FVIII) missense mutations remains unknown. Site-directed mutagenesis of B domain-deleted FVIII cDNA (FVIIISQ) was used to introduce two mutations associated with severe cross-reacting material (CRM)-negative (FVIII-C329S)

    Articles

    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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