MMP-13 (E3Q4Y) Rabbit mAb recognizes endogenous levels of total MMP-13 protein. This antibody detects a band of unknown origin at 28 kDa by western blot.

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of mouse MMP-13 protein.

MMP-13 (collagenase 3) belongs to the matrix metalloproteinase (MMP) superfamily of enzymes that targets many extracellular proteins, including other proteases, growth factors, cell surface receptors, and adhesion molecules (1,2). MMP-13 is a member of a subgroup of collagenases (including MMP-1, MMP-8, and MMP-18) that play an even more important function targeting fibrillar collagen. MMP-13 is synthesized as a latent proenzyme, and proteolytic removal of the inhibitory propeptide domain is required for enzyme activation. MMP-13 protein levels are regulated at the transcriptional level via specific transcription factors and promoter DNA methylation (3,4). MMP-13 preferentially cleaves Type II collagen, and research studies have shown that aberrant upregulation of MMP-13 activity can lead to cartilage loss and osteoarthritis (5,6). In addition, MMP-13 has been shown to promote cancer development, in part through enhancing tumor angiogenesis and metastases (7-9), suggesting that collagenase activity may serve as a useful marker of tumor progression (10).