ERAP2 Human Recombinant Protein

Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 (MIM 606832) and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2; MIM 190470) (Tanioka et al., 2003 [PubMed 12799365]).[supplied by OMIM, Mar 2008]

ERAP2: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys. Belongs to the peptidase M1 family. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Protease; EC 3.4.11.-; Endoplasmic reticulum

Chromosomal Location of Human Ortholog: 5q15

Cellular Component: endoplasmic reticulum membrane; endoplasmic reticulum lumen; integral to membrane

Molecular Function: metallopeptidase activity; zinc ion binding; aminopeptidase activity

Biological Process: antigen processing and presentation of peptide antigen via MHC class I; regulation of blood pressure; proteolysis; antigen processing and presentation of endogenous peptide antigen via MHC class I