Anti-ATP7B Antibody Picoband® Fluoro488 Conjugated

ATPase, Cu++ transporting, beta polypeptide (Wilson disease) protein, also called ATP7B, is an ATPase that transports copper. This gene is a member of the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least two putative copper-binding sites. ATP7B is mapped to 13q14.3. This protein functions as a monomer, exporting copper out of the cells. When copper levels are in excess, ATP7B redistributes to a vesicular compartment near the biliary canalicular membranes for elimination of excess copper into bile, and it is transported along liver cell microtubules via interaction with the p62 dynactin subunit.

Serine/threonine-protein kinase/endoribonuclease IRE1; Endoplasmic reticulum-to-nucleus signaling 1; Inositol-requiring protein 1; hIRE1p; Ire1-alpha; IRE1a; Serine/threonine-protein kinase; Endoribonuclease; ERN1

Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis.

1. Entrez Gene: ATP7B ATPase, Cu++ transporting, beta polypeptide. 2. Lim, C. M., Cater, M. A., Mercer, J. F. B., La Fontaine, S. Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A. J. Biol. Chem. 281: 14006-14014, 2006.