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 Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].
MMP2
Origin: Human
Host: HEK-293 Cells
Recombinant
The purity of the protein is greater than 85 % as determined by SDS-PAGE and Coomassie blue staining.
Lei, Gao, Liu, Liu, Wang: "Poly(glycidyl methacrylate-co-2-hydroxyethyl methacrylate) Brushes as Peptide/Protein Microarray Substrate for Improving Protein Binding and Functionality." in: ACS applied materials & interfaces, (2016) (PubMed).
Zheng, Hu, Huang, Xu, Yang, Li: "In vivo bioengineered ovarian tumors based on collagen, matrigel, alginate and agarose hydrogels: a comparative study." in: Biomedical materials (Bristol, England), Vol. 10, Issue 1, pp. 015016, (2015) (PubMed).
Wan, Han, Fan, Zhang, Gong, Sun: "Enzyme-responsive liposomes modified adenoviral vectors for enhanced tumor cell transduction and reduced immunogenicity." in: Biomaterials, Vol. 34, Issue 12, pp. 3020-30, (2013) (PubMed).