|Calculated MW||53820 Da|
|Other Names||Collagenase 3, 3424-, Matrix metalloproteinase-13, MMP-13, MMP13|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human MMP-13 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP-13 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Secreted, extracellular space, extracellular matrix. Secreted|
|Tissue Location||Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.|
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Provided below are standard protocols that you may find useful for product applications.
Collagenase-3 (MMP13), a member of the matrix metalloproteinase (MMP) family of neutral endopeptidases, is expressed in the skeleton during embryonic development and is highly overexpressed in human carcinomas and in chondrocytes and synovial cells in rheumatoid arthritis and osteoarthritis. Findings demonstrate a unique role of Mmp13 in skeletal development (1). In arthritis, the destruction of fibrillar (type II) collagen is one of the hallmarks, with MMP-1 and MMP-13 being identified as key players in arthritic cartilage. MMP-13, furthermore, has been found in highly metastatic tumors. In contrast to many human MMPs, the MMP-13 distribution pattern is restrictive in normal tissues and selective in pathological conditions. MMP-13 demonstrates versatility in its substrate utilization. In addition to being highly active on type II collagen, MMP-13 cleaves other substrates, mostly macromolecules of the extracellular matrix, but also molecules such as connective tissue (CTGF) and fibrinogen. MMP-13 is controlled at multiple levels: i.e., the expression/synthesis, activation, and inhibition of the active enzyme (3).
1. Inada M, et al. Proc Natl Acad Sci USA 101(49):17192-7, 2004
2. Maskos K, et al. J Mol Biol 366(4):1222-31, 2007.
3. Tardif G, et al. Mod Rheumatol 14(3):197-204, 2004
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