MMP-13
MMP-13 (matrix metallopeptidase 13, also known as collagenase 3 or CLG3) is a secreted peptidase of the M10A family that degrades extracellular matrix proteins. It cleaves triple helical collagens, with the highest activity towards soluble type II collagen. Browse Assay Genie's current range of MMP-13 research reagents below, or read on for the biology behind the target.
MMP-13 contributes to the breakdown of extracellular matrix proteins, including fibrillar collagen, fibronectin, TNC and ACAN. It cleaves triple helical type I, type II and type III collagen, with the highest activity on soluble type II collagen, and can also degrade collagen type IV, type XIV and type X. It may also act by activating or degrading regulatory proteins such as TGFB1 and CCN2.
The MMP13 gene encodes a member of the peptidase M10 family of matrix metalloproteinases and sits within a cluster of MMP genes on chromosome 11. The encoded preproprotein is proteolytically processed to generate the mature protease, which is secreted into the extracellular space and matrix. HGNC places it among the M10 matrix metallopeptidases, and the mouse and rat orthologs are both named Mmp13.
Functionally, MMP-13 is associated with wound healing, tissue remodelling, cartilage degradation, bone development, bone mineralisation and ossification. It is required for normal embryonic bone development and ossification, and contributes to bone fracture healing through endochondral ossification. In wound healing it appears to act through proteolytic activation of TGFB1 and degradation of CCN2, and it plays a role in keratinocyte migration. It may also take part in cell migration and tumour cell invasion.
The protein is a candidate contributor to articular cartilage turnover and to cartilage pathophysiology in osteoarthritis, and matrix metalloproteinases in general are implicated in arthritis and metastasis. Mutations in the gene are associated with metaphyseal anadysplasia. The gene was previously named matrix metalloproteinase 13 (collagenase 3).
MMP-13 cleaves type II collagen efficiently and may be involved in articular cartilage turnover and osteoarthritis pathophysiology.
It is required for normal embryonic bone development and ossification, and contributes to fracture healing via endochondral ossification.
MMP-13 supports keratinocyte migration and appears to act in wound healing through TGFB1 activation and CCN2 degradation.
As an extracellular matrix-degrading protease, MMP-13 may play a role in cell migration and tumour cell invasion.
MMP-13 is a secreted collagenase that degrades extracellular matrix components, including fibrillar collagen, fibronectin, TNC and ACAN. It cleaves type II collagen most efficiently and contributes to wound healing, tissue remodelling, cartilage degradation, bone development and ossification.
MMP-13 is the display name for the product of the MMP13 gene, formally matrix metallopeptidase 13. It is also called collagenase 3 or CLG3, and the gene was previously named matrix metalloproteinase 13 (collagenase 3). The protein belongs to the peptidase M10A family.
MMP-13 may contribute to cartilage pathophysiology in osteoarthritis, and mutations in the gene are associated with metaphyseal anadysplasia. Mouse and rat both have an ortholog named Mmp13; check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including collagenases, gelatinases and stromelysins, that act on extracellular matrix turnover.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P45452; product specifications from Assay Genie datasheets.