Anti-MMP13 Antibody Picoband®

Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs) . Proteins in this 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. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. Mutations in this gene are associated with metaphyseal anadysplasia. This gene is part of a cluster of MMP genes on chromosome 11.

Angiogenesis, Cancer, Cardiovascular, Cell Biology, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes, Signal Transduction, Tumor Biomarkers

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity) .

1. Bonafe, L., Liang, J., Gorna, M. W., Zhang, Q., Ha-Vinh, R., Campos-Xavier, A. B., Unger, S., Beckmann, J. S., Le Bechec, A., Stevenson, B., Giedion, A., Liu, X., Superti-Furga, G., Wang, W., Spahr, A., Superti-Furga, A. MMP13 mutations are the cause of recessive metaphyseal dysplasia, Spahr type. Am. J. Med. Genet. 164A: 1175-1179, 2014. 2. Freije, J. M. P., Diez-Itza, I., Balbin, M., Sanchez, L. M., Blasco, R., Tolivia, J., Lopez-Otin, C. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269: 16766-16773, 1994. 3. Inada, M., Wang, Y., Byrne, M. H., Rahman, M. U., Miyaura, C., Lopez-Otin, C., Krane, S. M. Critical roles for collagenase-3 (Mmp13) in development of growth plate cartilage and in endochondral ossification. Proc. Nat. Acad. Sci. 101: 17192-17197, 2004.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.