Matrix metalloproteinase-1, MMP-1, Human, Recombinant

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.

Fibroblast collagenase, Interstitial collagenase

E. Coli

MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEK AFQLWSNVTP LTFTKVSEGQ ADIMISFVRG DHRDNSPFDG PGGNLAHAFQ PGPGIGGDAH FDEDERWTNN FREYNLHRVA AHELGHSLGL SHSTDIGALM YPSYTFSGDV QLAQDDIDGI QAIYGRSQNP VQPIGPQTPK ACDSKLTFDA ITTIRGEVMFF KDRFYMRTNP FYPEVELNFI SVFWPQLPNG LEAAYEFADR DEVRFFKGNK YWAVQGQNVL HGYPKDIYSS FGFPRTVKHI DAALSEENTG KTYFFVANKY WRYDEYKRSM DPGYPKMIAH DFPGIGHKVD AVFMKDGFFY FFHGTRQYKF DPKTKRILTL QKANSWFNCR KN

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 ug/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes

Verified by N-terminal and Mass Spectrometry analyses (when applicable).