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MMP-12 (catalytic domain) (human), (recombinant)

BML-SE138-0010 10 µg 488.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 12, Metalloelastase, Macrophage elastase
MW:20.3 kDa
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.
UniProt ID:P39900
Formulation:Liquid. In 50mM TRIS, pH 9.5, containing 5mM calcium chloride, 500mM sodium chloride, 20µM zinc chloride, 0.5% Brij-35, and 30% glycerol.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Activity:Preincubation of MMP-12 catalytic domain at 4nM with the inhibitor NNGH (Prod. No. BML-PI115) at 20nM, or with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 5nM, for 1 hour completely inhibits enzymatic activity.
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.
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
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.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
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.
Regulatory Status:RUO - Research Use Only
MMP-12 (catalytic domain) (human), (recombinant) SDS-PAGE
SDS-PAGE Analysis: Lane1, MWM; Lane 2, 1.0 µg of purified human MMP-12 protein. In the SDS-PAGE gel, the enzyme runs as a doublet (~20kDa). 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.
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MMP-12 (catalytic domain) (human), (recombinant) SDS-PAGE

Product Literature References

MMP-12 polarizes neutrophil signalome towards an apoptotic signature: U. Chalise, et al.; J. Proteomics 264, 104636 (2022), Abstract;
Matrix Metalloproteinase MMP-12 promotes macrophage transmigration across intestinal epithelial tight junctions and increases severity of experimental colitis: M. Nighot, et al.; J. Crohns Colitis 64, 1093 (2021), Abstract;
Early Matrix Metalloproteinase-12 Inhibition Worsens Post-Myocardial Infarction Cardiac Dysfunction by Delaying Inflammation Resolution: R.P. Iyer, et al.; Int. J. Cardiol. 185, 198 (2015), Application(s): Cell Culture, Abstract;
The in vitro resistance of IgG2 to proteolytic attack concurs with a comparative paucity of autoantibodies against peptide analogs of the IgG2 hinge: R.J. Brezski, et al.; Mabs 3, 558 (2011), Abstract; Full Text
MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III: S. Taddese, et al.; Biochim. Biophys. Acta 1804, 731 (2010), Abstract;

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