342001

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.

• Enzyme Commission number: 3.4.22.38 (BRENDA, IUBMB)
• UNSPSC Code: 12352202

Properties

• recombinant: expressed in E. coli
• Quality Level: 100
• 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

Description

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 superfamiliy 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.

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.

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Physical form

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

Reconstitution

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).

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.

Legal Information

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

Safety Information

• Storage Class Code: 12 - Non Combustible Liquids
• WGK: WGK 2
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable