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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP3 is an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.
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. Stromelysin-1, also recognized as matrix metalloproteinase-3 (MMP-3), is an enzyme encoded by the MMP3 gene in humans. Aliases are: CHDS6, MMP-3, SL-1, STMY, STMY1, and STR1.This enzyme plays a significant role in the degradation of fibronectin, laminin, as well as collagens III, IV, IX, and X, along with cartilage proteoglycans. MMP-3 is involved in various biological processes such as wound repair, the progression of atherosclerosis, and the initiation of tumors.
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 estromelisina-1, también reconocida como metaloproteinasa de matriz-3 (MMP-3), es una enzima codificada por el gen MMP3 en humanos. Los alias son: CHDS6, MMP-3, SL-1, STMY, STMY1 y STR1. Esta enzima juega un papel importante en la degradación de la fibronectina, la laminina, así como los colágenos III, IV, IX y X, junto con el cartílago. proteoglicanos. MMP-3 participa en diversos procesos biológicos, como la reparación de heridas, la progresión de la aterosclerosis y la iniciación de tumores.
Primary Antibodies
Polyclonal
Human
Matrix Metalloproteinase 3 / Stromelysin-1 (MMP3)
Rabbit
Unconjugated
Liquid
ELISA, WB, IHC, FCM
Purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
PBS containing 0.09% sodium azide.
80 µl
400 µl
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
MMP3
No
Shipped within 5-10 working days.
This product is for research use only.
Stromelysin-1 Antibody (Biotin) is a Rabbit Polyclonal antibody against Stromelysin-1 conjugated to Biotin.
162.5€ (20 µg)
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