MMP-3 / Unconjugated / MMP3/2655

Product Details

Description	The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP3, MMP10 and MMP11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP3 activation of procollagenase can occur via two pathways. Direct activation by MMP3 is slow and activation by MMP3 in conjunction with tissue or plasma proteinases is rapid. MMP10 is expressed in small intestine, and at lower levels in lung and heart. MMP11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
Conjugate	Unconjugated
Clone	MMP3/2655
Target Species	Human
Applications	ELISA, WB
Supplier	NSJ Bioreagents
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About MMP-3
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 fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

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