Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava

antibody

MMP-9 Antibody

AB13458

500 µL

polyclonal

domestic rabbit

nonconjugated

western blot, immunohistochemistry, immunohistochemistry - paraffin section

Cell Structure

Anti-MMP-9 Antibody

Antibodies

Polyclonal Antibody

P14780

Rabbit

MMP-9

Purified

Anti-MMP-9 Antibody

Guinea Pig;Human

Matrix metalloproteinases (also named matrixin or MMPs) are a major group of enzymes that regulate cell-matrix composition by using zinc for their proteolytic activities. They are essential for various normal biological processes such as embryonic development, morphogenesis, reproduction tissue resorption, and remodeling. Metalloproteinases also play a role in pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and cancer. The metalloproteinase MMP-9 is associated with a variety of autoimmune diseases including systemic lupus erythematosus, Sjogren's syndrome, systemic sclerosis, rheumatoid arthritis, multiple sclerosis, polymyositis and atherosclerosis. MMP-9 plays either a primary or secondary role in each one of these autoimmune diseases by its up or down-regulation. It is not expressed constantly but rather is induced or suppressed by many regulating molecules. This feature of MMP-9 along with its involvement in disease pathogenesis turns it into a target for therapy in the treatment of potentially many autoimmune diseases. Like other proteolytic enzymes, MMP-9 is first synthesized as inactive proenzyme or zymogens. activation of proMMP-9 is mediated by plasminogen activator/plasmin (PA/plasmin) system. The regulation of MMP-9 activity is also controlled through TIMP-3. MMP-9 expression is regulated by several cytokines and growth factors, including interleukins, interferons, EGF, NGF, bFGF, VEGF, PDGF, TNF-alpha, TGF-beta, the extracellular matrix metalloproteinase inducer EMMPRIN and also osteopontin. Many of these stimuli induce the expression and/or activation of c-fos and c-jun proto-oncogene products, which heterodimerize and bind activator protein-1 (AP-1) sites within of MMP9 gene promoters. Normally MMP-9’s primary function is the degradation of the extracellular matrix. It can degrade decorin, elastin, fibrillin, laminin, gelatin (denatured collagen), and types IV, V, XI and XVI collagen and also activates growth factors like proTGF-beta and proTNF-alpha. Physiologically, MMP-9 in coordination with other MMPs, play a role in normal tissue remodeling events such as neurite gowth, embryonic development, angiogenesis, ovulation, mammary gland involution and wound healing. MMP-9 with other MMPs is also involved in osteoblastic bone formation and/or inhibits osteoclastic bone resorption. {http://atlasgeneticsoncology.org/Genes/MMP9ID41408ch20q11.html}.

92 kDa Type IV Collagenase;92 kDa gelatinase;Gelatinase B;GELB

Amino acids 626-644 of human MMP-9

AB13458 recognizes proteins of 92kDa and ~86kDa which are identified as pro (latent) and activated forms of matrix metalloproteinase 9 (MMP-9; also known as 92kDa collagenase IV or gelatinase B). CHEMICON AB13458 shows no cross-reaction with pro and active forms of other MMPs. CELLULAR LOCALIZATION:Enzyme is localized within the cytoplasm.

500 µL

Western Blotting;Immunohistochemistry;Immunohistochemistry (Paraffin)

Antibody is stable for 12 months after date of receipt when stored at 2-8 C.