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Merck

69671

Thrombin, Restriction Grade

Synonyme(s) :

Thrombin, Restriction Grade

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A propos de cet article

Numéro CAS:
9002-04-4
MDL number:
MFCD18251359
NACRES:
NA.54
UNSPSC Code:
12352202
Biological source:
human plasma

Principaux documents

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biological source

human plasma

form

liquid

manufacturer/tradename

Novagen®

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

technique(s)

protein extraction: suitable

suitability

suitable for additive or modifier in the separation of proteins or peptides

application(s)

life science and biopharma

shipped in

wet ice

storage temp.

−20°C

Quality Level

400

General description

Restriction Grade Thrombin is a highly purified preparation qualified to specifically cleave target proteins produced with appropriate vectors. This preparation is functionally tested for activity with fusion proteins and is free of detectable contaminating proteases. Prepared from human plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. Thrombin is supplied as a solution in 50% glycerol and includes 10X Thrombin Cleavage Buffer and a Cleavage Control Protein.

Preparation Note

Prepared from human plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Other Notes

•50 UThrombin

•1 ml10X Thrombin Cleavage Buffer

•2 ml1X Thrombin Dilution/Storage Buffer

•10 µgCleavage Control Protein
One unit is defined as the amount of enzyme needed to cleave 1 mg of fusion protein in 16 hours at 20°C in a 200 µl reaction containing 20 mM Tris-HCl pH 8.4, 150 mM NaCl, 2.5 mM CaCl₂, 50 µg fusion protein.

Legal Information

NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Multiple Toxicity Values, refer to MSDS (O)

Classe de stockage

10 - Combustible liquids

wgk

WGK 1

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Jooyoung Park et al.
eLife, 8 (2019-12-20)
The computational design of a symmetric protein homo-oligomer that binds a symmetry-matched small molecule larger than a metal ion has not yet been achieved. We used de novo protein design to create a homo-trimeric protein that binds the C3 symmetric
Christian M Smolko et al.
Scientific reports, 9(1), 19409-19409 (2019-12-21)
Protein kinases are enzymes whose abundance, protein-protein interactions, and posttranslational modifications together determine net signaling activity in cells. Large-scale data on cellular kinase activity are limited, because existing assays are cumbersome, poorly sensitive, low throughput, and restricted to measuring one

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