Additional information
| Qty | 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP3 - catalytic domain, inactive mutant
210,00€ – 680,00€
Human, recombinant
Residues 100-272, UniProtKB accession P08254
MW = 19.5 kDa
EC # 3.4.24.17
CAT # G04MP03Ci
| Catalog n. | Qty | Price |
|---|---|---|
| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
| VAT not included | ||
For any special request or bulk quantities Click Here
Description
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.
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.
Sequence
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.
> 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).
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 assay with thiopeptolide Ac-Pro-Leu- Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.
Not detected. Activity described as U=100 pmol/min at 25°C using a colorimetric assay 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.
Usage
Enzyme kinetic studies, and screening of inhibitors.
RELEATED RESEARCH FIELDS
- Biomaterials
- Cancer
- breast cancer
- lung cancer
- Dental diseases
- periodontitis
- pulpitis
- Neurodegenerative diseases
- Alzheimer’s disease
- Amyotrophic lateral sclerosis
- Multiple sclerosis
- Parkinson’s disease
- Osteoarthritis
- Renal pathologies
- chronic allograft nephropathy
- diabetic nephropathy
- glomerulosclerosis/tubulointerstitial fibrosis
- polycystic kidney disease
- renal cell carcinoma
- Tissue regeneration
- Wound healing
References
Johnson, L.L. et al. J. Biol. Chem. 275 (15), 11026-11033 (2000).
Chen, L. et al. J. Mol. Biol. 293 (3), 545-557 (1999).
Weingarten, H. & Feder, J. Anal. Biochem. 147 (2), 437-440 (1985).
Weingarten, H., Martin, R. & Feder, J. Biochemistry 24 (23), 6730-6734 (1985).
Chen, L. et al. J. Mol. Biol. 293 (3), 545-557 (1999).
Weingarten, H. & Feder, J. Anal. Biochem. 147 (2), 437-440 (1985).
Weingarten, H., Martin, R. & Feder, J. Biochemistry 24 (23), 6730-6734 (1985).