Additional information
| Qty | Custom quantity, 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP9 - catalytic domain
210,00€ – 680,00€
Human, recombinant
Residues 112-445, UniProtKB accession P14780
MW = 37.7 kDa
EC # 3.4.24.35
CAT # G04MP09C
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| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
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Description
Description
MW = 37.7 kDa calculated. Recombinant Matrix Metalloproteinase-9 (MMP-9, 92 kDa type IV collagenase, 92 kDa gelatinase, Gelatinase B, GELB) catalytic domain with fibronectin domains cloned from human cDNA, expressed in E. coli. The recombinant enzyme consists of the catalytic domain of human MMP-9 (residues 112-445, UniProtKB accession P14780) with a N-term T7 tag.
MW = 37.7 kDa calculated. Recombinant Matrix Metalloproteinase-9 (MMP-9, 92 kDa type IV collagenase, 92 kDa gelatinase, Gelatinase B, GELB) catalytic domain with fibronectin domains cloned from human cDNA, expressed in E. coli. The recombinant enzyme consists of the catalytic domain of human MMP-9 (residues 112-445, UniProtKB accession P14780) with a N-term T7 tag.
Sequence
120 130 140 150
MGRGSEF -GDLKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA
160 170 180 190 200
VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG
210 220 230 240 250
DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS YSACTTDGRS
260 270 280 290 300
DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS
310 320 330 340 350
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP
360 370 380 390 400
FTFLGKEYST CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA
410 420 430 440
HEFGHALGLD HSSVPEALMY PMYRFTEGPP LHKDDVNGIR HLYGP
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 35.0 and 45.0 kDa.
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 35.0 and 45.0 kDa.
Supplied as
0.15 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 5 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M, glycerol 10%, Brij35 0.05%. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 67100 M-1cm-1 calculated).
0.15 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 5 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M, glycerol 10%, Brij35 0.05%. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 67100 M-1cm-1 calculated).
Specific activity
> 10 U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric assay with thiopeptide 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, cleavage of target substrates and screening of inhibitors.
Releated research fiels
- Biomaterials
- Cancer
- breast cancer
- lung cancer
- pancreatic cancer
- prostate cancer
- Cardiovascular disorders
- aneurysm formation
- coronary artery disease
- myocardial infarction
- Dental diseases
- periodontitis
- pulpitis
- Diabetes Mellitus
- Neurodegenerative diseases
- Alzheimer’s disease
- Amyotrophic lateral sclerosis
- Huntington disease
- Multiple sclerosis
- Parkinson’s disease
- Renal pathologies
- chronic allograft nephropathy
- diabetic nephropathy
- glomerulosclerosis/tubulointerstitial fibrosis
- polycystic kidney disease
- renal cell carcinoma
- Tissue regeneration
- Wound healing
References
Ram, M., Sherer, Y. & Shoenfeld, Y. J. Clin. Immunol. 26 (4), 299-307 (2006).
Sawa, M. et al. J. Med. Chem. 45 (4), 930-936 (2002).
Bode, W. et al. Cell. Mol. Life Sci. 55 (4), 639-652 (1999).
Murphy, G. & Knäuper, V. Matrix Biol. 15 (8-9), 511-518 (1997).
Ram, M., Sherer, Y. & Shoenfeld, Y. J. Clin. Immunol. 26 (4), 299-307 (2006).
Sawa, M. et al. J. Med. Chem. 45 (4), 930-936 (2002).
Bode, W. et al. Cell. Mol. Life Sci. 55 (4), 639-652 (1999).
Murphy, G. & Knäuper, V. Matrix Biol. 15 (8-9), 511-518 (1997).