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. MMP17 is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMPs in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage.
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. MMP-17, also recognized as membrane-type matrix metalloproteinase 4 (MT-MMP 4), is an enzyme encoded by the MMP17 gene in humans. It is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) . High expression of this protein has been observed in conditions such as osteoarthritis and multiple human cancers. It also goes by aliases including MT4-MMP, MMP-17, MT4MMP, and MTMMP4.
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. MMP-17, también reconocida como metaloproteinasa 4 de matriz de tipo membrana (MT-MMP 4), es una enzima codificada por el gen MMP17 en humanos. Está anclado a la membrana celular mediante un anclaje de glicosilfosfatidilinositol (GPI). Se ha observado una expresión elevada de esta proteína en afecciones como la osteoartritis y múltiples cánceres humanos. También tiene alias que incluyen MT4-MMP, MMP-17, MT4MMP y MTMMP4.
Primary Antibodies
Polyclonal
Human
Matrix Metalloproteinase 17 (MMP17)
Rabbit
Unconjugated
Liquid
ELISA, WB, IHC
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.
MMP17
No
Shipped within 5-10 working days.
This product is for research use only.
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