This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down the interstitial collagens, including types I, II, and III. The gene is part of a cluster of MMP genes on chromosome 11. Mutations in this gene are associated with chronic obstructive pulmonary disease (COPD). Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
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. Interstitial collagenase, also recognized as matrix metalloproteinase-1 (MMP-1), is an enzyme encoded by the MMP1 gene in humans. This enzyme, when secreted, serves to degrade interstitial collagens, including types I, II, and III. It is also known by aliases such as CLG and CLGN
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 intersticial, también reconocida como metaloproteinasa de matriz-1 (MMP-1), es una enzima codificada por el gen MMP1 en humanos. Esta enzima, cuando se secreta, sirve para degradar los colágenos intersticiales, incluidos los tipos I, II y III. También se le conoce con alias como CLG y CLGN
Primary Antibodies
polyclonal
human,mouse,rat
matrix metallopeptidase 1 (interstitial collagenase)
Rabbit
IgG
Unconjugated
liquid
ELISA, WB, IHC
54 kDa
≥95% as determined by SDS-PAGE
Immunogen affinity purified
WB: 1:500 - 1:2000; IHC: 1:50 - 1:200
100µg
PBS with 0.02% sodium azide and 50% glycerol pH 7.3 , -20℃ for 12 months (Avoid repeated freeze / thaw cycles.)
MMP1
CLG, CLGN, Fibroblast collagenase, Interstitial collagenase, Matrix metalloproteinase 1, MMP 1, MMP1
This product is for research use only.
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