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MMP-13  Protein, Antibody, ELISA Kit, cDNA Clone

MMP-13 Related Area

MMP-13 Related Pathways

MMP-13 Summary & Protein Information

MMP-13 Background

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; ; Note=Can bind about 5 Ca(2+) ions per subunit.;; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; ; Note=Binds 2 Zn(2+) ions per subunit.;
Enzyme regulation: ENZYME REGULATION: Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited by acetohydroxamic acid and other zinc chelators. {ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.
Subunit structure: Monomer. Interacts with TIMP1, TIMP2 and TIMP3. Binds (via the C-terminal region) to collagen. {ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8969305, ECO:0000269|PubMed:9065415}.
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity). {ECO:0000250}.; The C-terminal region binds to collagen. {ECO:0000269|PubMed:9065415}.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:8576151}. Secreted {ECO:0000269|PubMed:8576151}.
Tissue specificity: 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. {ECO:0000269|PubMed:8207000, ECO:0000269|PubMed:8798568, ECO:0000269|PubMed:9056642, ECO:0000269|PubMed:9562863}.
Induction: Up-regulated by TNF and IL1B. {ECO:0000269|PubMed:8798568, ECO:0000269|PubMed:9056642}.
Post-translational: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).; N-glycosylated. {ECO:0000269|PubMed:8576151}.; Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000269|PubMed:25171405}.
Involvement in disease: DISEASE: Spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [MIM:602111]: A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age. {ECO:0000269|PubMed:16167086}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metaphyseal anadysplasia 1 (MANDP1) [MIM:602111]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarity: Belongs to the peptidase M10A family. {ECO:0000305}.; Contains 4 hemopexin repeats. {ECO:0000305}.
General information above from UniProt

MMP-13 Alternative Name

MMP-13 Related Studies

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