ERAP1
ERAP1 (endoplasmic reticulum aminopeptidase 1, also known as ARTS-1, A-LAP, PILS-AP, KIAA0525 and ERAAP1) is an M1 family aminopeptidase that trims peptide precursors in the endoplasmic reticulum. This trimming step is required for the generation of most HLA class I-binding peptides. Browse Assay Genie's current range of ERAP1 research reagents below, or read on for the biology behind the target.
ERAP1 is an aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Longer precursor peptides must be customised to the correct length before they can be presented on MHC class I molecules, and the ERAP1 protein carries out this shortening. It strongly prefers substrates 9-16 residues long and rapidly degrades a 13-mer to a 9-mer, then stops. It preferentially hydrolyses the residue Leu and peptides with a hydrophobic C-terminus, and has weak activity towards peptides with a charged C-terminus.
The enzyme belongs to the peptidase M1 family and sits in the HGNC gene groups for aminopeptidases, minor histocompatibility antigens and M1 metallopeptidases. It is located at the endoplasmic reticulum membrane. According to the NCBI Gene summary, the encoded protein acts as a monomer or as a heterodimer with ERAP2, and the ERAP1 gene produces three transcript variants encoding two different isoforms. Mouse and rat each have an orthologous Erap1 gene.
Beyond antigen processing, ERAP1 may play a role in the inactivation of peptide hormones. It may also be involved in the regulation of blood pressure, through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. The alias ARTS-1, along with A-LAP, PILS-AP, KIAA0525 and ERAAP1, appears across the literature, so searches for an ERAP1 antibody, ERAP1 ELISA kit or related reagent often need to account for these names.
ERAP1 trims precursor peptides to the length needed for presentation on MHC class I molecules, making it central to HLA class I peptide generation.
The enzyme strongly prefers substrates of 9-16 residues and rapidly degrades a 13-mer to a 9-mer before stopping, which suits studies of peptide length.
ERAP1 may regulate blood pressure by inactivating angiotensin II and/or generating bradykinin in the kidney.
ERAP1 acts as a monomer or as a heterodimer with ERAP2, so the pair is of interest in studies of cooperative peptide trimming.
ERAP1 is an aminopeptidase that trims precursor peptides so they fit the length required for presentation on MHC class I molecules. It prefers substrates 9-16 residues long and favours Leu and hydrophobic C-termini. It may also inactivate peptide hormones and contribute to blood pressure regulation.
ERAP1 is also called ARTS-1, A-LAP, PILS-AP, KIAA0525 and ERAAP1. The official name is endoplasmic reticulum aminopeptidase 1. NCBI reports three transcript variants for the gene, which encode two different isoforms of the protein.
Yes. Mouse and rat both carry an orthologous gene named Erap1. ERAP1 can function as a monomer or as a heterodimer with ERAP2. Check the datasheet of any product for its validated reactivity.
ERAP2, the heterodimer partner of ERAP1, is a related antigen-processing aminopeptidase with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9NZ08; product specifications from Assay Genie datasheets.