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Safety Information

T6884

Sigma-Aldrich

Thrombin from human plasma

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

Synonym(s):

Factor IIa

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CN¥1,673.87
250 UNITS
CN¥3,336.19
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100 UNITS
CN¥1,673.87
250 UNITS
CN¥3,336.19
1000 UNITS
CN¥7,960.99
5000 UNITS
CN¥35,932.79

About This Item

CAS Number:
9002-04-4
Enzyme Commission number:
3.4.21.5 (BRENDA, IUBMB)
EC Number:
232-648-7
MDL number:
MFCD00082072
UNSPSC Code:
12352204
NACRES:
NA.54

CN¥1,673.87

Available to ship onApril 14, 2025Details

Request a Bulk Order

biological source

human plasma

Quality Level

200

form

lyophilized powder

specific activity

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

mol wt

37.4 kDa

impurities

HIV and HBsAg, source material tested negative

UniProt accession no.

P00734

storage temp.

−20°C

Gene Information

human ... F2(2147)

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1 of 4

This Item
T1063T4393T7009
Thrombin from human plasma lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280, 18.3)

T6884

Thrombin from human plasma

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

T1063

Thrombin from human plasma

Thrombin from human plasma lyophilized powder, 1500-3500 NIH units/mg protein (E1%/280, 18.3), suitable for cell culture

T4393

Thrombin from human plasma

Thrombin from human plasma lyophilized powder, ≥1,000 NIH units/mg protein (E1%/280, 18.3)

T7009

Thrombin from human plasma

specific activity

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

specific activity

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

specific activity

1500-3500 NIH units/mg protein (E1%/280, 18.3)

specific activity

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

biological source

human plasma

biological source

-

biological source

human plasma

biological source

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

UniProt accession no.

P00734

UniProt accession no.

P00734

UniProt accession no.

P00734

UniProt accession no.

P00734

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

Thrombin is produced from the proteolytic cleavage of inactive prothrombin in the liver.[1] It is a glycoprotein with four structural domains: the 10 γ-carboxylated glutamic acid containing Gal domain, two kringle domains, and the trypsin-like serine protease domain.[2] The prothrombin gene is mapped to human chromosome 11p11.2.[1]
Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects.

Application

Thrombin from human plasma has been used:
  • in the preparation of fibrin gels for assessing human bone marrow stromal cells (hBMSC) morphology[3],
  • in the activation of platelets[4],
  • to evaluate the integrity of endothelial cell (EC) monolayers[5]

Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags.

Biochem/physiol Actions

Serine protease that selectively cleaves Arg-Gly bonds in fibrinogen to form fibrin and fibrinopeptides A and B.
The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation.[6] A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia.[1] High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease.[7] Altered thrombin levels modulates the coagulation pathway in multiple sclerosis.[8] Patients with coronary artery disease (CAD) show elevated levels of thrombin.[9] Thrombin accumulation in neurofibrillary tangles of the brain may contribute to the aggregation of tau protein and pathophysiology of Alzheimer disease.[10]
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 investigate the protein C pathway in intestinal barrier function. [11]

Unit Definition

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

Physical form

Lyophilized from saline sodium citrate buffer, pH 6.5

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.

inhibitor

Product No.
Description
Pricing

substrate

Product No.
Description
Pricing

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品
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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000383376
    0000383376
    0000416265
    0000416265
    0000410300

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    1. Which document(s) contains shelf-life or expiration date information for a given product?

      If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

    2. How do I get lot-specific information or a Certificate of Analysis?

      The lot specific COA document can be found by entering the lot number above under the "Documents" section.

    3. Can a stock solution of Product T6884, Thrombin, be stored frozen?

      A suggested stock solution is 100 units/ml. The solution should contain 0.1% BSA for stability and may be stable for about one week at 0-5°C. Since thrombin solutions adsorb to glass, it is recommended to aliquot the solutions in plastic tubes and store at -20°C or below.

    4. How do I find price and availability?

      There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

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    Howard Kim et al.
    PloS one, 6(6), e21744-e21744 (2011-07-09)
    Neural stem/progenitor cells (NSPCs) have great potential as a cell replacement therapy for spinal cord injury. However, poor control over transplant cell differentiation and survival remain major obstacles. In this study, we asked whether dibutyryl cyclic-AMP (dbcAMP), which was shown
    Substrate stiffness combined with hepatocyte growth factor modulates endothelial cell behavior
    Chang H, et al.
    Biomacromolecules, 17(9), 2767-2776 (2016)
    Platelet subpopulations remain despite strong dual agonist stimulation and can be characterised using a novel six-colour flow cytometry protocol
    Sodergren ALand Ramstrom S
    Scientific reports, 8(1), 1441-1441 (2018)
    Silvia D'Alessio et al.
    Annals of the New York Academy of Sciences, 1258, 78-85 (2012-06-27)
    The protein C (PC) pathway is a well-characterized anticoagulant system. Produced mainly by the liver as a zymogen, PC is activated on the vascular endothelial cell surface by thrombin-thrombomodulin complex. Once activated, PC inactivates two important cofactors of the coagulation
    Effect of the scaffold microenvironment on cell polarizability and capacitance determined by probabilistic computations
    Betancourt BA, et al.
    Bio-medical materials and engineering, 13(2), 025012-025012 (2018)
    View All Related Papers

    Articles

    Thrombin Factor IIa

    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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