Description
General description
50 μg protein, determined by Bradford. For the lot-specific concentration, see Certificate of Analysis.
Recombinant human Matrix Metalloproteinase-9 (MMP-9) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 76 kDa (amino acids 20-707). The DTT-reduced protein migrates as a ~92 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.
Biochem/physiol Actions
MMP-9 is a member of the matrix metalloproteinase (MMP) family of proteins. Proteins of the MMP family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Studies in rhesus monkeys suggest that MMP9 is involved in IL-8 (interleukin-8)-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Thrombospondins, intervertebral disc proteins, regulate the effective levels of MMP-2 and -9, which are key effectors of extracellular matrix (ECM) remodeling. MMP-9 degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 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.
MMP-9 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.
Structurally, MMP9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain.
Physical form
Liquid solution, 0.22 mm filtered, containing 25 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35
Other Notes
This product can be activated in vitro by adding 4-Aminophenylmercuric acetate (APMA), Cat. No. A9563, to a final concentration of 1 mM.
