ERAP1 (K467) polyclonal antibody

The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) is a 120 kDa protein localized to the lumen of the ER, which removes NH2-terminal residues from many antigenic precursors for MHC class I peptide presentation. Peptides that are presented by MHC class I on the surface of a cell must be 8-11 residues long, and ERAP1 specifically trims peptides of 9 amino acids or more. ERAP1 is also induced by interferon-γ. The gene encoding human ERAP1 maps to chromosome 5q15. ERAP1 has previously been characterized as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1) . A-LAP is thought to inactivate several bioactive peptides, including angiotensin II and, subsequently, may be involved in the regulation of blood pressure. PILS-AP is described as playing a role in angiogenesis by regulating the proliferation and migration of endothelial cells, and ARTS-1 is characterized as a TNFR1 binding protein that promotes TNFR1 shedding. Further research will be necessary to fully elucidate the functions of this protein.

Endoplasmic reticulum aminopeptidase 1; ARTS-1; Adipocyte-derived leucine aminopeptidase; A-LAP; Aminopeptidase PILS; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator; ERAP1; APPILS; ARTS1, KIAA0525; UNQ584/PRO1154

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of ERAP1 (K467) pAb at 1:500 dilution Lane1:HepG2 whole cell lysate (40ug) Lane2:HEK293T whole cell lysate (20ug) Lane3:PC12 whole cell lysate (20ug) Lane4:AML-12 whole cell lysate (40ug)