342001

Procathepsin K, Human, Recombinant, E. coli

Name: Procathepsin K, Human, Recombinant, <i>E. coli</i>
Brand: MM

Recombinant, human procathepsin K expressed in E. coli with a methionine residue inserted at amino acid 18 to create a new N-terminal initiation site.

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About This Item

EC Number:

3.4.22.38 (BRENDA, IUBMB)

NACRES:

NA.77

UNSPSC Code:

12352202

Product Name

Procathepsin K, Human, Recombinant, E. coli, Recombinant, human procathepsin K expressed in E. coli with a methionine residue inserted at amino acid 18 to create a new N-terminal initiation site.

recombinant

expressed in E. coli

assay

≥95% (SDS-PAGE)

form

liquid

specific activity

≥1000 mU/mg protein

manufacturer/tradename

Calbiochem^®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

shipped in

wet ice

storage temp.

−70°C

Quality Level

100

Disclaimer

Toxicity: Standard Handling (A)

General description

If the activated enzyme is not used immediately, it is recommended to add methyl methanthiosulfonate (1 mM final concentration MMTS).

Note: 1 mU = 1 milliunit.

Recombinant, human procathepsin K (amino acids 19-329) (GenBank target symbol = S79895, ACC No. P43235) expressed in E. coli with a methionine residue inserted at amino acid 18 to create a new N-terminal initiation site. Cathepsin K, a member of the papain superfamily of cysteine proteinases, plays an important role in osteoclast-mediated bone resorption and collagen degradation. Cathepsin K is synthesized as an inactive proenzyme that is converted to its mature, active form by proteolytic cleavage of the 99 amino acid propeptide domain. Inhibitors of cathepsin K include leupeptin (Cat. No. 108975) (IC₅₀ = 70 nM), E-64 (Cat. No. 324890) (IC₅₀ = 5 nM), and cystatin (Cat. No. 324891 or 324896). Requires activation prior to use.

Other Notes

McQueney, M., et al. 1997. J. Bio. Chem.272, 13955.
Bossard, M., et al. 1996. J. Biol. Chem.271, 12517.
Drake, F., et al. 1996. J. Biol. Chem.271, 12511.
Bromme, D. and Okamoto, K. 1995. Biol. Chem. Hoppe-Seyler376, 379.
Baron, R. 1989 Anat. Rec.224, 317.
Littlewood-Evans, A.J., et al. 1975. Cancer Res.57, 5386.
Nishimura, J.S. et al. 1975. Arch. Biochem. Biophys.170, 461.

One unit is defined as the amount of enzyme that will hydrolyze 1 µmole benzyloxycarbonyl-phenylalanine-arginine-7-amido-4-methylcoumarin per min at 37°C, pH 5.5.

Packaging

Please refer to vial label for lot-specific concentration.

Physical form

In 500 mM NaCl, 25 mM Tris, pH 8.0.

Preparation Note

Following initial thaw, aliquot and freeze (-70°C). Following activation the enzyme is unstable and should include MMTS for storage (see recommended reaction conditions for activation).

Legal Information

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

Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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