Recombinant Human MMP-2
Catalog Number : 420-02
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-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Above 90% as determined by SDS-PAGE Analysis.
MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.
MYNFFPRKP KWDKNQITY RIIGYTPDL DPETVDDAF ARAFQVWSD VTPLRFSRI HDGEADIMI NFGRWEHGD GYPFDGKDG LLAHAFAPG TGVGGDSHF DDDELWTLG EGQVVRVKY GNADGEYCK FPFLFNGKE YNSCTDTGR SDGFLWCST TYNFEKDGK YGFCPHEAL FTMGGNAEG QPCKFPFRF QGTSYDSCT TEGRTDGYR WCGTTEDYD RDKKYGFCP ETAMSTVGG NSEGAPCVF PFTFLGNKY ESCTSAGRS DGKMWCATT ANYDDDRKW GFCPDQGYS LFLVAAHEF GHAMGLEHS QDPGALMAP IYTYTKNFR LSQDDIKGI QELYGASPD IDLGTGPTP TLGPVTPEI CKQDIVFDG IAQIRGEIF FFKDRFIWR TVTPRDKPM GPLLVATFW PELPEKIDA VYEAPQEEK AVFFAGNEY WIYSASTLE RGYPKPLTS LGLPPDVQR VDAAFNWSK NKKTYIFAG DKFWRYNEV KKKMDPGFP KLIADAWNA IPDNLDAVV DLQGGGHSY FFKGAYYLK LENQSLKSV KFGSIKSDW LGC
|Research Interest:||Cancer, Angiogenesis, Bone Biology|
|Protein Cross Reactivity:||NULL|