The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application notesWB: 1/1000 for using colorimetric substrates such as BCIP/NBT. WB: 1/5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. Predicted molecular weight: 84 kDa. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
FunctionMembrane metallopeptidase that sheds many membrane-bound proteins. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.
Tissue specificityThe major site of expression is the brush border membrane of small intestinal and kidney epithelial cells.
Sequence similaritiesBelongs to the peptidase M12A family. Contains 1 EGF-like domain. Contains 1 MAM domain. Contains 1 MATH domain.
Post-translational modificationsN-glycosylated; contains high mannose and/or complex biantennary structures. O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human. Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.
Cellular localizationCell membrane. Secreted. Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.