MMP-1

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.

Matrix metalloproteinase-1, fibroblast collagenase, interstitial collagenase

4312

P03956

NP_002412.1

NM_002421.3

11q22.3

Human

Human

MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEKAF QLWSNVTPLT FTKVSEGQAD IMISFVRGDH RDNSPFDGPG GNLAHAFQPG PGIGGDAHFD EDERWTNNFR EYNLHRVAAH ELGHSLGLSH STDIGALMYP SYTFSGDVQL AQDDIDGIQA IYGRSQNPVQ PIGPQTPKAC DSKLTFDAIT TIRGEVMFFK DRFYMRTNPF YPEVELNFIS VFWPQLPNGL EAAYEFADRD EVRFFKGNKY WAVQGQNVLH GYPKDIYSSF GFPRTVKHID AALSEENTGK TYFFVANKYW RYDEYKRSMD PGYPKMIAHD FPGIGHKVDA VFMKDGFFYF FHGTRQYKFD PKTKRILTLQ KANSWFNCRK N

< 0.1 ng/µg of protein (< 1EU/µg)

> 90% by SDS-PAGE & HPLC 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

371

Lyophilized

42.7 kDa

E. coli