Active Recombinant Human MMP14 protein, mutation C127S
Cat.No. : | MMP14-33H |
Product Overview : | Recombinant Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase1, MT1- MMP) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-14 (residues 114-290, UniProtKB accession P50281). The protein has the mutation C127S to increase its stability. The catalytic activity rates are not affected by the mutation. |
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Species : | Human |
Source : | Non |
Protein Length : | 114-290 aa |
Tag : | Non |
Bio-activity : | > 150 U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric assay with thiopeptide Ac-Pro-Leu-Gly-[2- mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate. |
Molecular Mass : | 20.1 kDa |
AA Sequence : | IQGLKWQ HNEITFSIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIGGDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP |
Purity : | > 95% by SDS-PAGE |
Usage : | Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors. |
Storage : | -80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C. Avoid repeated freeze/thaw cycles. |
Storage Buffer : | 0.2 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M. |
GeneID : | 4323 |
References : | M. Gioia et al. J Mol Biol. 2007 May 11;368(4):1101-13. K. Lehti et al. J. Biol. Chem. 2000, 275:15006-13. G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 511. W. Bode et al. Cell Mol Life Sci 1999, 55:639-52. |
Gene Name | MMP14 matrix metallopeptidase 14 [ Homo sapiens (human) ] |
Official Symbol | MMP14 |
Synonyms | MMP-14,MMP-X1,MT-MMP,MT1MMP,MTMMP1,WNCHRS,MT1-MMP,MT-MMP 1,MMP14 |
mRNA Refseq | NM_004995 |
Protein Refseq | NP_004986 |
MIM | 600754 |
UniProt ID | P50281 |
◆ Recombinant Proteins | ||
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◆ Cell & Tissue Lysates | ||
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Not For Human Consumption!
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