Proximpsin K; Human ; recombinate ; e. coli

Code: 342001-10ug D2-231

Non disponible en dehors du Royaume-Uni et de l'Irlande

General description

Note: 1 mU = 1 milliunit.

Recombinant, human procathepsin K (amino acids 19-329) (GenBank target symbol = S79895, ACC No. P43235) expressed in E...


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£327.00 10UG

Non disponible en dehors du Royaume-Uni et de l'Irlande

General description

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.

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.

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

Legal Information

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

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.

Packaging

10 µg in Plastic ampoule

Please refer to vial label for lot-specific concentration.

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).

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.

Warning

Toxicity: Standard Handling (A)

assay≥95% (SDS-PAGE)
formliquid
manufacturer/tradenameCalbiochem®
Quality Level100
recombinantexpressed in E. coli
shipped inwet ice
specific activity≥1000 mU/mg protein
storage conditionavoid repeated freeze/thaw cycles, OK to freeze
storage temp.−70°C
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