Function
Functions both as a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised.
Biological Context
Subcellular Location: Periplasm
Product Specifications
Recombinant Escherichia coli Beta-barrel assembly-enhancing protease (bepA) is a recombinant protein from Escherichia coli (strain K12), expressed in E.coli, covering amino acids 28-487aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 58.5kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Protease proteins →
