MMP-15/MT2-MMP Products

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. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Bioinformatics

Entrez	4324 Human
Product By Gene ID	4324
Alternate Names	EC 3.4.24 EC 3.4.24.- EC 3.4.24.80 matrix metallopeptidase 15 (membrane-inserted) matrix metalloproteinase 15 (membrane-inserted) Membrane-type matrix metalloproteinase 2 Membrane-type-2 matrix metalloproteinase MMP15 MMP-15 MT2-MMP MT2-MMPMT2MMP MTMMP2MT-MMP 2 SMCP-2matrix metalloproteinase-15

Research Areas for MMP-15/MT2-MMP

Find related products by research area and learn more about each of the different research areas below.

Extracellular Matrix