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219461

Cathepsin K, His•Tag®, Human, Recombinant, E. coli

Cathepsin K, His•Tag, Human, Recombinant, E. coli, CAS 94716-09-3, of the papain superfamily of cysteine proteinases plays a role in osteoclast-mediated bone resorption and collagen degradation.

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Rozmiar/SKUDostępnośćCena netto
25 μg

Przewidywana wysyłka DZISIAJzKuehne + Nagel Sp. z o.o.

1420,00 zł

Informacje o tej pozycji

Numer CAS:
94716-09-3
Numer WE:
3.4.22.38 (BRENDA, IUBMB)
NACRES:
NA.77
UNSPSC Code:
12352202
MDL number:
MFCD00011084
eCl@ss:
32035490
Form:
liquid
Assay:
≥95% (SDS-PAGE)
Recombinant:
expressed in E. coli

1420,00 zł

Przewidywana wysyłka DZISIAJSzczegóły

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recombinant

expressed in E. coli

Quality Segment

assay

≥95% (SDS-PAGE)

form

liquid

specific activity

≥900 mU/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

shipped in

wet ice

storage temp.

−70°C

General description

Cathepsin K is a member of the papain superfamily of cysteine proteinases and plays an important role in osteoclast-mediated bone resorption and collagen degradation. It is primarily expressed by osteoclasts and recent studies also suggest its expression in fibroblasts. Irregularities in cathepsin K activity, either too high or too low, contribute to osteopenic disorders such as osteoporosis and pycnodysostosis. This recombinant enzyme contains a C-terminal His•Tag sequence.
Note: 1 mU = 1 milliunit.

Packaging

Please refer to vial label for lot-specific concentration.

Physical form

In 50 mM NaOAC, pH 5.5. The activation was stopped by addition of 10 mM MMTS, which can be removed under reducing conditions.

Preparation Note

Following initial thaw, aliquot and freeze (-70°C).

Other Notes

Delaisse, J.M., et al. 2003. Microsc. Res. Tech.61, 504.
Dodds, R.A. 2003. Cell Biochem. Funct.21, 231.
Everts, V., et al. 2003. Calcif. Tissue Int.73, 380.
Hou, W.S., et al. 2003. Biol. Chem.384, 891.
One unit is defined as the amount of enzyme that will hydrolyze 0.4 µmol Z-FR-AMC per min at 37°C, pH 5.5.

Legal Information

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

Disclaimer

Toxicity: Standard Handling (A)
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Ta pozycja
219343208670499260
Cathepsin K, His•Tag®, Human, Recombinant, E. coli Cathepsin K, His•Tag, Human, Recombinant, E. coli, CAS 94716-09-3, of the papain superfamily of cysteine proteinases plays a role in osteoclast-mediated bone resorption and collagen degradation.

Sigma-Aldrich

219461

Cathepsin K, His•Tag®, Human, Recombinant, E. coli

Cathepsin S, Human, Recombinant, E. coli Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity.

Sigma-Aldrich

219343

Cathepsin S, Human, Recombinant, E. coli

Kalmodulina, His-Tag® ludzki, rekombinowany Calmodulin, His•Tag Human, Recombinant, is a full-length, recombinant human calmodulin fused to a His•Tag sequence at the N-terminus. Contains four functional Ca2+-binding sites.

Sigma-Aldrich

208670

Kalmodulina, His-Tag® ludzki, rekombinowany

Osteopontyna, His-Tag®, Mysz, rekombinowana, Mysz

Sigma-Aldrich

499260

Osteopontyna, His-Tag®, Mysz, rekombinowana, Mysz

description

Cathepsin K, His•Tag, Human, Recombinant, E. coli, CAS 94716-09-3, of the papain superfamily of cysteine proteinases plays a role in osteoclast-mediated bone resorption and collagen degradation.

description

Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity.

description

Calmodulin, His•Tag Human, Recombinant, is a full-length, recombinant human calmodulin fused to a His•Tag sequence at the N-terminus. Contains four functional Ca2+-binding sites.

description

-

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

-

assay

≥95% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

>90% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

liquid

form

liquid

form

liquid

form

lyophilized

specific activity

≥900 mU/mg protein

specific activity

≥30,000 mU/mg protein

specific activity

-

specific activity

-

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage condition

avoid repeated freeze/thaw cycles, OK to freeze

storage condition

avoid repeated freeze/thaw cycles, OK to freeze

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze

Klasa składowania

12 - Non Combustible Liquids

WGK

nwg

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Certyfikaty analizy (CoA)

Lot/Batch Number

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