Direkt zum Inhalt
Merck

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.

Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise


About This Item

EC-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.77

Rekombinant

expressed in E. coli

Qualitätsniveau

Assay

≥95% (SDS-PAGE)

Form

liquid

Spezifische Aktivität

≥1000 mU/mg protein

Hersteller/Markenname

Calbiochem®

Lagerbedingungen

OK to freeze
avoid repeated freeze/thaw cycles

Versandbedingung

wet ice

Lagertemp.

−70°C

Allgemeine Beschreibung

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.

Verpackung

Please refer to vial label for lot-specific concentration.

Warnhinweis

Toxicity: Standard Handling (A)

Einheitendefinition

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.

Physikalische Form

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

Rekonstituierung

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).

Sonstige Hinweise

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.

Rechtliche Hinweise

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

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung.