Product Name :
MMP-12 (catalytic domain) (human), (recombinant)
Sequence:
Purity:
≥95% (SDS-PAGE)
Molecular Weight:
20.3 kDa
Solubility :
Appearance:
Use/Stability :
The enzyme is stable on ice for at least several hours. However, it is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. When stored per recommendation, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.
Description:
CAS :
Solubility:
Formula:
Additional Information :
| Activity Preincubation of MMP-12 catalytic domain at 4nM with the inhibitor NNGH at 20nM, or with the broad-spectrum inhibitor GM6001 at 5nM, for 1 hour completely inhibits enzymatic activity.{{1628323-80-7} web|{1628323-80-7} Protocol|{1628323-80-7} Purity|{1628323-80-7} custom synthesis} | Alternative Name Matrix metalloproteinase 12, Metalloelastase, Macrophage elastase | Application Notes Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. | Formulation Liquid. In 50mM TRIS, pH 9.5, containing 5mM calcium chloride, 500mM sodium chloride, 20µM zinc chloride, 0.{{339177-26-3} MedChemExpress|{339177-26-3} Protocol|{339177-26-3} Formula|{339177-26-3} custom synthesis} 5% Brij-35, and 30% glycerol.PMID:30521273 | MW 20.3 kDa | Purity ≥95% (SDS-PAGE) | Purity Detail Purified by multi-step chromatography. | Source Produced in E. coli. Active Matrix Metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase; often confused with neutrophil elastase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-12 (Phe99-Leu271, NM_002426) with a C-terminal purification tag. | Specific Activity ≥2000 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate. | Technical Info / Product Notes In an SDS-PAGE gel, the enzyme runs as a doublet (~20 kDa). The higher band represents the polypeptide described above, while spontaneous cleavage of the tag results in the lower band. Both species possess identical enzymatic activities. | UniProt ID P39900
