- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
The MEP1B antibody targets Meprin A subunit beta, a zinc metalloprotease encoded by the MEP1B gene. This enzyme is a member of the astacin family of metalloproteases and plays a key role in extracellular matrix remodeling, proteolytic processing of bioactive molecules, and epithelial homeostasis. Meprin A subunit beta combines with Meprin A subunit alpha or forms homodimers to generate active protease complexes localized at the plasma membrane. The MEP1B antibody provides researchers with a reliable means to study this protease's structure, function, and contribution to physiological and pathological processes.
Meprin A subunit beta is synthesized as a zymogen and activated through proteolytic cleavage. Once active, it catalyzes the hydrolysis of various substrates, including extracellular matrix proteins such as collagen, fibronectin, and laminin, as well as cytokines and growth factors. These activities make Meprin A subunit beta a crucial regulator of tissue remodeling and inflammatory signaling. The MEP1B antibody allows scientists to detect this enzyme in epithelial cells, intestinal mucosa, and kidney proximal tubules, where it plays essential roles in maintaining barrier function and proteolytic balance.
Mutations or altered expression of MEP1B have been linked to inflammatory bowel disease, fibrosis, and cancer. Overexpression may enhance degradation of matrix components, facilitating tumor invasion or chronic tissue injury, while loss of function can impair epithelial integrity. The MEP1B antibody enables evaluation of these changes in expression patterns, helping clarify the connection between Meprin A subunit beta and disease pathology. Recent studies also suggest Meprin B's involvement in activation of interleukin precursors and complement components, further extending its biological significance.
At the molecular level, Meprin A subunit beta anchors to the plasma membrane via a transmembrane domain, orienting its catalytic site extracellularly. It interacts with glycoproteins and proteoglycans that influence its enzymatic specificity and activity. The MEP1B antibody is an effective tool for studying these protein�protein interactions using western blotting, immunohistochemistry, and immunofluorescence. Researchers frequently apply it in tissue-based assays to evaluate distribution and regulation in kidney, intestine, and liver, where the enzyme's expression is most prominent.
Beyond normal physiology, Meprin A subunit beta has drawn attention for its potential contribution to neurodegenerative and fibrotic disorders. Proteolytic imbalance caused by excess Meprin activity can exacerbate inflammatory cascades and extracellular matrix turnover. The MEP1B antibody from NSJ Bioreagents allows reproducible and sensitive detection, supporting investigations into protease-mediated signaling and tissue remodeling. Through consistent performance across experimental applications, this reagent assists in advancing understanding of how metalloprotease activity shapes health and disease.
Optimal dilution of the MEP1B antibody should be determined by the researcher.
E.coli-derived human MEP1B recombinant protein (Position: H73-Q489) was used as the immunogen for the MEP1B antibody.
After reconstitution, the MEP1B antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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