Skip to Content
Merck

T4648

Thrombin from bovine plasma

lyophilized powder, 40-500 NIH units/mg protein (biuret)

Synonym(s):

Factor IIa

Sign In to View Organizational & Contract Pricing.

Select a Size

About This Item

CAS Number:
9002-04-4
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-648-7
MDL number:
MFCD00166053
EC Number:
3.4.21.5 (BRENDA, IUBMB)
Specific activity:
40-500 NIH units/mg protein (biuret)
Biological source:
bovine plasma

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Quality Level

300

biological source

bovine plasma

form

lyophilized powder

specific activity

40-500 NIH units/mg protein (biuret)

mol wt

heavy chain ~33 kDa, light chain ~5 kDa

composition

Protein, 40-60%

Gene Information

cow ... F2(280685)

color

, white to faint yellow to faint red

UniProt accession no.

P00735

shipped in

wet ice

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

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 assess persistent hypocoagulability in patients with septic shock.

Biochem/physiol Actions

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

Physical form

Lyophilized powder containing sodium chloride and Tris-HCl, pH 7.0

Preparation Note

Activated with bovine brain thromboplastin.

Analysis Note

Activity is expressed in NIH units obtained by direct comparison to a NIH Thrombin Reference Standard, Lot K.
The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL 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

Activity is expressed in NIH units obtained by direct comparison to a NIH thrombin reference standard.
View more information on thrombin at www.sigma-aldrich.com/enzymeexplorer.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

T4648-1KU: + T4648-BULK: + T4648-100KU: + T4648-VAR: + T4648-10KU:

jan

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
SLBW2056
SLBZ5705
SLCC1592
SLBX8914
SLBX8909

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Persistent hypocoagulability in patients with septic shock predicts greater hospital mortality: impact of impaired thrombin generation
Massion, P., et al.
Intensive Care Medicine, 1823(8), 1316-1323 (2012)
Marek R Baranowski et al.
Nucleic acids research, 48(15), 8209-8224 (2020-06-10)
The high sensitivity of 19F nucleus to changes in the chemical environment has promoted the use of fluorine-labeled molecular probes to study structure and interactions of nucleic acids by 19F NMR. So far, most efforts have focused on incorporating the
Adam M Jorgensen et al.
Tissue engineering. Part A, 26(9-10), 512-526 (2019-12-22)
Over 1 million burn injuries are treated annually in the United States, and current tissue engineered skin fails to meet the need for full-thickness replacement. Bioprinting technology has allowed fabrication of full-thickness skin and has demonstrated the ability to close
Navid Hakimi et al.
Lab on a chip, 18(10), 1440-1451 (2018-04-18)
We present a handheld skin printer that enables the in situ formation of biomaterial and skin tissue sheets of different homogeneous and architected compositions. When manually positioned above a target surface, the compact instrument (weight <0.8 kg) conformally deposits a
Suping Li et al.
Nature biotechnology, 36(3), 258-264 (2018-02-13)
Nanoscale robots have potential as intelligent drug delivery systems that respond to molecular triggers. Using DNA origami we constructed an autonomous DNA robot programmed to transport payloads and present them specifically in tumors. Our nanorobot is functionalized on the outside
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service