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MilliporeSigma™ anti-MMP-7 Clone: 141-7B2,

Mouse Monoclonal Antibody

Supplier:  MilliporeSigma™ IM40100UG

Catalog No. IM40100UG


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Description

Description

Specifically detects MMP-7 Clone: 141-7B2 in Human samples, and it is validated for Immunohistochemistry (Paraffin)

The matrix metalloproteinases (MMP's) are a family of enzymes responsible for the degradation of extracellular matrix components. Of the eleven proteins reported to date, ten are normally found as soluble molecules. MMP-7, also known as matrilysin, is responsible for hydrolyzing proteoglycans and extracellular matrix glycoproteins and was first described in 1980 but not purified to homogeneity until 1988. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. The enzyme exists as an inactive pro form with a molecular weight of ∽28kDa (range: 28-30kDa) which becomes activated by proteolytic cleavage to an active 19kDa form. Pro-MMP-7 may be activated by trypsin, mercurial compounds or by MMP-3 and once activated can itself activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is distinguished from the other MMP family members as being the smallest member containing only the common catalytic domain and the Zn2+ binding region but missing the hemopexin-like domain common to the other MMP's. Matrilysin is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and in ∽50% of gliomas.
TRUSTED_SUSTAINABILITY
Specifications

Specifications

MMP-7
Monoclonal
Unconjugated
Mouse
100 μg
Primary
Human
Purified
Immunohistochemistry (Paraffin)
141-7B2
In 100mM sodium phosphate buffer, 0.1% BSA, pH 7.0.
human rectal carcinoma MMP-7
RUO
Recognizes the ∽28kDa latent form of MMP-7 in TPA-treated SW620 cells. Does not recognize the active form of MMP-7.
−20°C
IgG1
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