Anti-MEP1B Antibody Picoband® Fluoro488 Conjugated

Meprin A subunit beta is a protein that in humans is encoded by the MEP1B gene. Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes, and in leukocytes and certain cancer cells. They are involved in the hydrolysis of a variety of peptide and protein substrates, and have been implicated in cancer and intestinal inflammation. Mature meprins are oligomers of evolutionarily related, but separately encoded alpha and/or beta subunits. Homooligomers of alpha subunit are secreted, whereas, oligomers containing the beta subunit are plasma membrane-bound. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in kidney and intestine.

E.coli-derived human MEP1B recombinant protein (Position: H73-Q489) . Human MEP1B shares 82.3% and 81.5% amino acid (aa) sequence identity with mouse and rat MEP1B, respectively.

1. Bond, J. S., Rojas, K., Overhauser, J., Zoghbi, H. Y., Jiang, W. The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively. Genomics 25: 300-303, 1995. 2. Crisman, J. M., Zhang, B., Norman, L. P., Bond, J. S. Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. J. Immun. 172: 4510-4519, 2004. 3. Gorbea, C. M., Marchand, P., Jiang, W., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Bond, J. S. Cloning, expression, and chromosomal localization of the mouse meprin beta subunit. J. Biol. Chem. 268: 21035-21043, 1993.