MMP-9 / CLG4B Protein (Native)

Matrix Metalloproteinase-9 ( MMP-9 / CLG4B ) Protein

MMP-9 / CLG4B Protein Product Information

• Synonym: MMP9 , CLG4B , GELB , MMP-9
• Protein Construction: A DNA sequence encoding the human MMP9 zymogen ( NP_004985.2 ) ( Met 1 - Asp 707 ) was expressed
• Source: Human
• Expression Host: Human Cells

MMP-9 / CLG4B Protein QC Testing

• Purity: > 94 % as determined by SDS-PAGE
• Bio-activity: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 , (AnaSpec , Cat#27076)
  The specific activity is > 600 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 recombinant human MMP9 consisting of 688 amino acids has a predicted molecular mass of 76.3 kDa. The apparent molecular mass of rh MMP9 is approximately 80 - 95 kDa in SDS-PAGE due to glycosylation
• Formulation: Lyophilized from sterile 50mM Tris , 0.15M NaCl , 0.01M CaCl₂ , 0.05% Brig-35 , pH 7.5
  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: MMP9 protein

MMP-9 / CLG4B 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.

MMP-9 / CLG4B 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: 3581-3584.
2. Opdenakker, G. et al., 2001, J. Leuko. Biol. 69: 851-859.
3. Belotti, D. et al., 2003, Cancer. Res. 63: 5224-5229.
4. Mira, E. et al., 2004, J. Cell. Sci. 117:1847-1857.
5. Ram, M. et al., 2006, J. Clin. Immunol. 26: 299-307.