Anti-ERAP1 Antibody

The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1), a member of the peptidase M1 family, plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides (1,2) . It is also designated as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1) (3) . ERAP1 is localized to the lumen of the ER and induced by interferon. It may be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (3,4) .

ERAP1 antibody is human and mouse reactive. At least two isoforms of ERAP1 are known to exist; this antibody will detect both isoforms. ERAP1 antibody is predicted to not cross-react with ERAP2.

ERAP1 antibody was raised against a 19 amino acid peptide near the carboxy terminus of human ERAP. The immunogen is located within amino acids 730 - 780 of ERAP1 .

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. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.