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342001

Sigma-Aldrich

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.

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About This Item

Classificazione EC (Enzyme Commission):
Codice UNSPSC:
12352202
NACRES:
NA.77

Ricombinante

expressed in E. coli

Livello qualitativo

Saggio

≥95% (SDS-PAGE)

Stato

liquid

Attività specifica

≥1000 mU/mg protein

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

OK to freeze
avoid repeated freeze/thaw cycles

Condizioni di spedizione

wet ice

Temperatura di conservazione

−70°C

Descrizione generale

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.

Confezionamento

Please refer to vial label for lot-specific concentration.

Attenzione

Toxicity: Standard Handling (A)

Definizione di unità

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.

Stato fisico

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

Ricostituzione

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).

Altre note

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.

Note legali

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

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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