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. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.It can detect the glycosylated proMMP-13(70 kDa), unglycosylated proform(54 kDa).
MMPs are secreted by diverse connective tissue and pro-inflammatory cells. Typically, these enzymes exhibit minimal expression under normal physiological circumstances. MMPs assume a pivotal role in various cellular processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and immunity. They share a common domain structure, consisting of three key components. First is the pro-peptide, which requires removal to activate the enzyme. Next, there is the catalytic domain, featuring a cysteine switch, where a cysteine residue interacts with zinc, and the haemopexin-like C-terminal domain is linked to the catalytic domain via a flexible hinge region. Collagenase 3, also known as MMP-13, is an enzyme encoded by the MMP13 gene in humans. It is also recognized by its aliases CLG3, MANDP1, and MDST. MMP-13 is particularly efficient at cleaving type II collagen, more so than types I and III. It is thought to be involved in the turnover of articular cartilage and is associated with the pathophysiology of osteoarthritis. The activity of MMP-13 is tightly regulated due to its potent proteolytic capabilities. Various cytokines and growth factors have been shown to influence the expression of the Mmp13 gene, including parathyroid hormone, IGF-1, TGF-β, hepatocyte growth factor, as well as several inflammatory cytokines such as IL-1α and IL-1β.
MMPs son secretadas por diversos tejidos conectivos y células proinflamatorias. Normalmente, estas enzimas exhiben una expresión mínima en circunstancias fisiológicas normales. Las MMP asumen un papel fundamental en diversos procesos celulares, incluida la proliferación, migración, diferenciación, angiogénesis, apoptosis e inmunidad celular. Comparten una estructura de dominio común, que consta de tres componentes clave. El primero es el propéptido, que requiere eliminación para activar la enzima. A continuación, está el dominio catalítico, que presenta un interruptor de cisteína, donde un residuo de cisteína interactúa con el zinc, y el dominio C-terminal similar a hemopexina está unido al dominio catalítico a través de una región bisagra flexible. La colagenasa 3, también conocida como MMP-13, es una enzima codificada por el gen MMP13 en humanos. También se le reconoce por sus alias CLG3, MANDP1 y MDST. MMP-13 es particularmente eficaz para escindir el colágeno tipo II, más que los tipos I y III. Se cree que participa en la renovación del cartílago articular y está asociado con la fisiopatología de la osteoartritis. La actividad de MMP-13 está estrictamente regulada debido a sus potentes capacidades proteolíticas. Se ha demostrado que varias citocinas y factores de crecimiento influyen en la expresión del gen Mmp13, incluida la hormona paratiroidea, IGF-1, TGF-β, factor de crecimiento de hepatocitos, así como varias citocinas inflamatorias como IL-1α e IL-1β.
Primary Antibodies
polyclonal
human,mouse,rat
matrix metallopeptidase 13(collagenase 3)
Rabbit
IgG
Unconjugated
liquid
ELISA, IHC, WB, IF
54kd,70kd
≥95% as determined by SDS-PAGE
Immunogen affinity purified
WB: 1:500-1:1000; IHC: 1:20-1:200; IF: 1:10-1:100
100µg
PBS with 0.02% sodium azide and 50% glycerol pH 7.3,-20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
MMP13
CLG3, Collagenase 3, Matrix metalloproteinase 13, MMP 13, MMP13
This product is for research use only.
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