||Recombinant Human Hemopexin-Like Domain (C domain) of MMP2, from human cDNA, was expressed inE. coli. The protein consists of the hemopexin-like domain of human MMP-2. (residues 467-660, swissprot accession P08253 ). MW = 22.2 kDa.
||Proteins of the matrix metalloproteinase (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. Most MMP"s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Torg-Winchester syndrome.
||> 95% by SDS-PAGE. The protein was observed as a single band migrating at amolecular weight of (>20 kDa).
||0.2mg/ml in 20mM Sodium Acetate, pH 5.5, 1mM CaCl2, 250mM NaCl. The concentration is calculated from the absorbance at 280nm (e280 = 51350 M-1 cm-1).
||Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated to a maximum of 150μM.
||-20ºC. After initial defrost, aliquot product into individual tubes and refreeze at -20ºC. Avoid repeated freeze/defrost cycles.