• Human MMP-13 protein (Recombinant) (C-His) (STJP000993)
  • Human MMP-13 protein (Recombinant) (C-His) (STJP000993)
  • Human MMP-13 protein (Recombinant) (C-His) (STJP000993)
  • Human MMP-13 protein (Recombinant) (C-His) (STJP000993)

Human MMP-13 protein (Recombinant) (C-His) (STJP000993)

SKU:
STJP000993

Current Stock:
Host: HEK293 cells
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Human MMP-13-C-His protein was developed from hek293 cells and has a target region of C-His. For use in research applications.
Formulation: Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4. Contact us for customized product form or formulation.
Immunoreactivity: Measured in a cell migration assay using A549 cells.10 ng/mL of Recombinant Human MMP-13 can effectively induce A549 cells migration.2. Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2. The specific activity is
Gene Symbol: MMP13
Gene ID: 4322
Uniprot ID: MMP13_HUMAN
Immunogen Region: Leu20-Cys471
Immunogen: Recombinant Human MMP-13 Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Leu20-Cys471) of human MMP-13 (Accession #NP_002418.1) fused with a 6×His tag at the C-terminus.
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.
Post Translational Modifications 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. Tyrosine phosphorylated by PKDCC/VLK.
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 CCN2. 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 CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
Protein Name Collagenase 3
Matrix Metalloproteinase-13
Mmp-13
Database Links Reactome: R-HSA-1442490
Reactome: R-HSA-1474228
Reactome: R-HSA-1592389
Reactome: R-HSA-2022090
Reactome: R-HSA-8941332
Cellular Localisation Secreted
Extracellular Space
Extracellular Matrix
Alternative Protein Names Collagenase 3 protein
Matrix Metalloproteinase-13 protein
Mmp-13 protein
MMP13 protein

Information sourced from Uniprot.org

12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance