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

 
BML-SE138-0010 10 µg 371.00 USD
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Product Specification

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:≥30 U/µg. One U=100 pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100µM; Prod. No. BML-P125) as substrate.
 
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on 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.
 
BML-SE138 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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BML-SE138 SDS-PAGE

Product Literature References

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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