GenWay/MMP-13/GWB-A9152D/0.01 mg-蚂蚁淘在线

Concentration: 70 ug/ml A DNA sequence (NM_002427) encoding full-length human mmp-13 enzyme (471 aa) was expressed in CHO cells.The matrix metalloproteinases (MMPs) constitute a family of zinc-dependent endopeptidases thatfunction within the extra cellular matrix. These enzymes are responsible for the breakdown of connective tissues and are important in bone remodeling, menstrual cycle and the repair of tissue damage.MMP-13 (collagenase-3),1 is a member of the MMP family of extra cellular proteases. The cDNA encodes a polypeptide of 471 amino acids. The predicted protein sequence displays extensive similarity to the previously known MMPs and presents all the structural features characteristic of the members of this protein family, including the well conserved PRCGXPD motif, involved in the latency of the enzyme and the zinc-binding domain (HEXGHXXXXXHS). In addition, MMP-13 contains in its amino acid sequence several residues specific to the collagenase subfamily (Tyr-214, Asp-235, and Gly-237) and lacks the 9-residue insertion present in the stromelysins (Freije J.M. et al., 1994). MMP-13 is able to degrade fibrillar collagens. The expression of MMP-13 in osteoarthritic cartilage and its activity against type II collagen suggest that the enzyme plays a significant role in cartilage collagen degradation (Mitchell P.G. et al., 1996)Targets of MMP-13 include collagen, gelatin, aggracan, plasminogen and CXCL12. The native MMP-13 is secreted as a 60-kDa proenzyme, and activated by cleavage to a mature 48-kDa MMP-13.Recombinant human MMP-13 (471 aa) was expressed as a pro-enzyme from its DNA sequence in CHO cells. The recombinant MMP-13 can be activated through incubation with 1 mM APMA at 37º C for 40 min. Its activity can be measured in FRET-based enzymatic assays (AnaSpec: Cat#71135, Cat#71156)Function: Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process.Cofactor: Binds 4 calcium ions per subunit.Cofactor: Binds 2 zinc ions per subunit.Subcellular Location: Secreted, extracellular space, extracellular matrix (Probable).Tissue Specificity: Seems to be specific to breast carcinomas.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.Disease: Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2) [MIM:602111]; also known as spondyloepimetaphyseal dysplasia type Missouri. SEMDs are a heterogeneous group of skeletal disorders characterized by defective growth and modeling of the spine and long bones. The SEMDs are distinguished from the spondylometaphyseal dysplasias and the spondyloepiphyseal dysplasias by the combined involvement of the epiphyses and metaphyses. The 3 disorders have malformations of the vertebrae in common.Similarity: Belongs to the peptidase M10A family [view classification].Similarity: Contains 4 hemopexin-like domains.