MMP-9 / CLG4B Antibody

Matrix Metalloproteinase 9 ( MMP9 ) Antibody Datasheet

MMP9 / CLG4B Antibody Product Information

• Immunogen: Recombinant human MMP-9 protein ( Catalog #10327-H08H )
• Antibody Type: Rabbit Polyclonal Antibody ( Antibody Purification Platform )
• Ig Type: Rabbit IgG
• Formulation: 0.2 μm filtered solution in PBS with 5% trehalose
• Preparation: Produced in rabbits immunized with purified, human cell-derived, recombinant human matrix metallopeptidase 9 ( rhMMP9; Catalog #10327-H08H; aa 1 - 707; NP_004985.2 ). Total IgG was purified by Protein A affinity chromatography.

MMP9 / CLG4B Antibody Usage Guide

• Specificity: Human MMP9 / CLG4B
• Western blot: This antibody can be used at 0.25-1μg/mL with the appropriate secondary reagents to detect human MMP9 in WB.
• Direct ELISA: This antibody can be used at 0.25-0.5μg/mL with the appropriate secondary reagents to detect human MMP9. The detection limit for human MMP9 is approximately 0.6 ng/well
• Storage: This antibody can be stored at 2℃-8℃ for 1 month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
  Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

MMP9 / CLG4B Antibody Background

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