Anti-MMP7 antibody produced in rabbit

NA.41

Matrix metallopeptidase 7 (matrilysin, uterine) (MMP7) is an extracellular matrix remodeling enzyme that catalyzes the degradation of interstitial proteoglycans such as fibronectin, elastin and casein. As a remodeling enzyme, MMP7 is involved in normal physiological processes such as embryonic development, reproduction, tissue remodeling and wound healing. MMP7 is also involved in diseases that involve matrix remodeling or destruction such as arthritis and tumor metastasis.

Anti-MMP7 polyclonal antibody reacts with bovine and human matrix metallopeptidase 7 proteins.

Synthetic peptide directed towards the C terminal region of human MMP7

Anti-MMP7 polyclonal antibody is used to tag matrix metallopeptidase 7 for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of matrix metallopeptidase 7 in matrix remodeling in both normal and pathological processes such as metastasis.

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. MMP7 degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa.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. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Synthetic peptide located within the following region: AATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGK

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

rabbit

100

unconjugated

IgG fraction of antiserum

primary antibodies

polyclonal

19 kDa

sheep, human

0.5 mg - 1 mg/mL

western blot: suitable

NP_002414

P09237

wet ice

−20℃

human ... MMP7(4316)

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