Rat MMP-9 / CLG4B Protein (His Tag)

Rat Matrix Metalloproteinase-9 Protein

Rat MMP-9 Protein Product Information

• Synonym: Mmp9
• Protein Construction: A DNA sequence encoding the rat MMP9 ( EDL96479.1 ) ( Met 1 - Pro 708 ) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Rat
• Expression Host: Human Cells

Rat MMP-9 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE
• Bio-activity: Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2, ( R&D Systems, Catalog # ES010 )
  The specific activity is > 1000 pmoles / min / µg
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ala 20
• Molecular Mass: The secreted recombinant rat MMP9 comprises 700 amino acids and predicts a molecular mass of 77.8 kDa. The apparent molecular mass of the rat MMP9 is approximately 100-110 kDa in SDS-PAGE under reducing conditions due to glycosylation
• Formulation: Lyophilized from sterile 50 mM MES, 100mM NaCl, 1mM CaCl2, 10% Glycerol, pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: MMP-9 protein

Rat MMP-9 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Rat MMP-9 Protein Description

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMPs are synthesized as enzymogen and converted to active form by other MMPs or extracellular proteinases. MMP-9/MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It contains a fibronectin-like domain, which functions in the binding of gelatin, a unique serine/proline/threonine-rich collagen type V-like domain probably serving as attachment sites of multiple O-linked oligosaccharides and a carboxyl terminal hemopexin-like domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. Studies have shown that MMP-9/MMP9 play control roles in IL8-induced leukocytosis and stem cell mobilization, and additionally in release of biologically active VEGF and consequently in the formation of ascites. MMP-9/MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.

References

1. Ogata, Y. et al., 1992, J. Biol. Chem. 267: 3581-4.
2. Reponen P., et al.,1994, J. Cell Biol. 124:1091-1102.
3. Opdenakker, G. et al., 2001, J. Leuko. Biol. 69: 851-9.
4. Belotti, D. et al., 2003, Cancer. Res. 63: 5224-9.
5. Mira, E. et al., 2004, J. Cell. Sci. 117:1847-57.
6. Ram, M. et al., 2006, J. Clin. Immunol. 26: 299-307.