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Key Documents

CC1059

Sigma-Aldrich

MMP-7, human, recombinant active form

Sinónimos:

Matrilysin

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About This Item

UNSPSC Code:
12352204
eCl@ss:
32160405
NACRES:
NA.41

biological source

human

Quality Level

form

liquid

specific activity

5,000 units/mg protein

manufacturer/tradename

Chemicon®

concentration

0.1 mg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

General description

MOLECULAR WT:

19,130 calculated from amino acid sequence and 20,000 from SDS-PAGE, followed by staining with CBB R-250.
Product Source: Recombinant E. Coli; prepared from recombinant human promatrilysin

Unit Definition

Specific Activity: One unit of enzyme activity is defined as the quantity required to digest 1 μg of Azocoll/min.at pH 7.5 and 37°C in the presence of 0.5 mM p-aminophenylmercuric acetate.

Physical form

Solution in 10 mM HEPES (pH 7.4)-5 mM CaCl2-0.15 M NaCl.

Storage and Stability

Maintain at -80ºC for up to one year.

Legal Information

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Tristen V Tellman et al.
International journal of molecular sciences, 22(6) (2021-04-04)
The Perlecan-Semaphorin 3A-Plexin A1-Neuropilin-1 (PSPN) Complex at the cell surface of prostate cancer (PCa) cells influences cell-cell cohesion and dyscohesion. We investigated matrix metalloproteinase-7/matrilysin (MMP-7)'s ability to digest components of the PSPN Complex in bone metastatic PCa cells using in

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