Proteins of the matrix metalloproteinase (MMP) 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes a secreted enzyme which breaks down the interstitial collagens, types I, II, and III. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants.
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
Matrix Metalloproteinase 1 (MMP1)
Rabbit
Unconjugated
Liquid
ELISA, WB, IHC, IF/ICC
Purified through a protein A column, followed by peptide affinity purification.
PBS containing 0.09% sodium azide.
80 µl
400 µl
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
MMP1
No
Shipped within 5-10 working days.
This product is for research use only.
Rabbit Polyclonal against the MMP1 protein.
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