Anti-ERAP1 Antibody

Endoplasmic reticulum aminopeptidase 1 (ERAP1) is a zinc-dependent metalloaminopeptidase resident in the ER lumen that trims precursor peptides to the optimal 8-10 mer length for loading onto MHC class I molecules, shaping the CD8+ T cell repertoire. This unconjugated rabbit polyclonal reagent from Antibodies.com is raised against ERAP1 and is validated across Western blot, immunohistochemistry, immunofluorescence, and ELISA workflows, with demonstrated reactivity against human, mouse, and rat samples. The antibody is supplied as 100 µl of polyclonal sera, unconjugated for flexible secondary antibody pairing and direct labeling in custom assay development. ERAP1 is widely investigated in antigen processing studies, in cancer immunotherapy research where altered peptide trimming affects tumor antigen presentation, and in autoimmune disease genetics, particularly ankylosing spondylitis and Behcet's disease where ERAP1 variants modulate disease risk. Researchers studying MHC class I antigen presentation, peptide trimming kinetics, or ER-resident aminopeptidase biology will find this reagent useful for tracking endogenous ERAP1 expression across tissue panels and cell models.