Recombinant Human MMP-1
Catalog Number : 420-01
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain which is involved in substrate specificity and in binding TIMP-1.
Above 90% as determined by SDS-PAGE Analysis.
MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes
MFVLTEGNP RWEQTHLTY RIENYTPDL PRADVDHAI EKAFQLWSN VTPLTFTKV SEGQADIMI SFVRGDHRD NSPFDGPGG NLAHAFQPG PGIGGDAHF DEDERWTNN FREYNLHRV AAHELGHSL GLSHSTDIG ALMYPSYTF SGDVQLAQD DIDGIQAIY GRSQNPVQP IGPQTPKAC DSKLTFDAI TTIRGEVMF FKDRFYMRT NPFYPEVEL NFISVFWPQ LPNGLEAAY EFADRDEVR FFKGNKYWA VQGQNVLHG YPKDIYSSF GFPRTVKHI DAALSEENT GKTYFFVAN KYWRYDEYK RSMDPGYPK MIAHDFPGI GHKVDAVFM KDGFFYFFH GTRQYKFDP KTKRILTLQ KANSWFNCR KN
|Research Interest:||Cancer, Angiogenesis, Bone Biology|
|Protein Cross Reactivity:||NULL|