Recombinant humaan MMP-3 eiwit

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP3 is an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. Recombinant human MMP3 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Matrix metallopeptidase 3, CHDS6, MMP-3, SL-1, STMY, STMY1, STR1

E.coli

Human

His-Tag

SDS-PAGE

0.25 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

45.2 kDa (401aa) confirmed by MALDI-TOF

MMP3, Matrix metallopeptidase 3, CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, ATGP2576-10 µg, ATGP2576-20 µg, ATGP2576-50 µg, ATGP2576-100 µg, ATGP2576-250 µg, ATGP2576-500 µg, ATGP2576-1 mg, ATGP2576-10, ATGP2576-20, ATGP2576-50, ATGP2576-100, ATGP2576-250, ATGP2576-500, ATGP2576-1

Nagase H., et al. (1990) Biochemistry. 29:5783-5789; ; Ye S., et al. (1996) J. Biol. Chem. 271:13055-13060;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 10% glycerol

Cancer

NP_002413

P08254

Human

MGSSHHHHHH SSGLVPRGSH MGSFRTFPGI PKWRKTHLTY RIVNYTPDLP KDAVDSAVEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVR EHGDFYPFDG PGNVLAHAYA PGPGINGDAH FDDDEQWTKD TTGTNLFLVA AHEIGHSLGL FHSANTEALM YPLYHSLTDL TRFRLSQDDI NGIQSLYGPP PDSPETPLVP TEPVPPEPGT PANCDPALSF DAVSTLRGEI LIFKDRHFWR KSLRKLEPEL HLISSFWPSL PSGVDAAYEV TSKDLVFIFK GNQFWAIRGN EVRAGYPRGI HTLGFPPTVR KIDAAISDKE KNKTYFFVED KYWRFDEKRN SMEPGFPKQI AEDFPGIDSK IDAVFEEFGF FYFFTGSSQL EFDPNAKKVT HTLKSNSWLN C