MMP26
MMP26 (matrix metallopeptidase 26, also known as endometase) is a secreted member of the M10 matrix metallopeptidase group that may degrade several extracellular matrix proteins. It can also activate progelatinase B, linking it to matrix breakdown and tissue remodelling. Browse Assay Genie's current range of MMP26 research reagents below, or read on for the biology behind the target.
MMP26 is a matrix metalloproteinase, a family of enzymes involved in the breakdown of extracellular matrix in normal physiological processes such as embryonic development, reproduction and tissue remodelling, as well as in disease processes such as arthritis and metastasis. UniProt annotates MMP26 as an enzyme that may hydrolyse collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. It is also able to activate progelatinase B, the precursor of MMP-9, by cleavage.
The MMP26 gene encodes a preproprotein that is proteolytically processed to generate the mature enzyme. The protein is secreted and found in the extracellular space and extracellular matrix. It belongs to the peptidase M10A family and to the HGNC group of M10 matrix metallopeptidases. MMP26 differs from most MMP family members in that it lacks a conserved C-terminal protein domain, a feature that sets its structure apart from many related MMPs.
The gene has also been described as matrix metalloproteinase 26, and the protein is commonly called endometase; MGC126590 and MGC126592 are older symbols. According to the RefSeq summary, the encoded protein may promote cell invasion in multiple human cancers, which makes MMP26 a point of interest for studies of matrix degradation and tumour biology. Researchers studying the MMP26 protein, or looking for an MMP26 antibody or MMP26 ELISA kit, will find it alongside other MMP family targets.
MMP26 may degrade collagen type IV, fibronectin and fibrinogen, so it is relevant to studies of matrix turnover in development, reproduction and tissue remodelling.
The encoded protein may promote cell invasion in multiple human cancers, making it a candidate for research into metastasis and matrix degradation.
MMP26 can activate progelatinase B by cleavage, placing it within proteolytic cascades that involve MMP-9.
Lacking the conserved C-terminal domain found in most MMPs, MMP26 is useful for comparing structure and function across the M10A family.
MMP26 is a secreted matrix metalloproteinase that may hydrolyse collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. It can also activate progelatinase B (MMP-9) by cleavage, contributing to extracellular matrix breakdown and remodelling.
MMP26 is also called endometase, and its previous name was matrix metalloproteinase 26. Older symbols include MGC126590 and MGC126592. HGNC lists the gene as matrix metallopeptidase 26 within the M10 matrix metallopeptidases group, and UniProt names the protein Matrix metalloproteinase-26.
MMP26 lacks a conserved C-terminal protein domain present in most MMP family members. NCBI Gene notes that it may promote cell invasion in multiple human cancers. Ortholog information is not given in the source data, so check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including the gelatinase MMP-9 that MMP26 can activate, and further M10 family members with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9NRE1; product specifications from Assay Genie datasheets.