MMP3 - catalytic domain, inactive mutant[产品打印页面]

Description
MW = 18.0 kDa. Recombinant matrix metalloproteinase-3 (MMP-3, stromelysin-1, transin) cloned from human cDNA, expressed in E.coli. The enzyme consists of the catalytic domain of human MMP-3, residues 105-265 (UniProtKB accession P08254). The enzyme has been inactivated by mutagenesis (E219A). This product is derived from MMP-3 Catalytic domain, and contain also the mutation F171D to increase its stability. No residual enzyme activity has been detected using the method described in the specific activity section of this data sheet.

                                        100        110        120
                                        M-F RTFPGIPKWR KTHLTYRIVN
       130        140        150        160        170        180
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD DYPFDGPGNV
       190        200        210        220        230        240
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHAI GHSLGLFHSA NTEALMYPLY
       250        260   265
HSLTDLTRFR LSQDDINGIQ SLYGP

Purity
> 95% by SDS-PAGE. The enzyme was observed as a single band migrating at a molecular weight of < 20 kDa.

Supplied as
0.2 mg/mL solution in Tris 20 mM, pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.2 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 28420 M-1cm-1 calculated).

Specific activity
Not detected. Activity described as U=100 pmol/min at 25°C using a colorimetric ***** with thiopeptolide Ac-Pro-Leu- Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.

Storage
-80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C.
Avoid repeated freeze/thaw cycles.