| Endoplasmic reticulum aminopeptidase 1 ELISA Kit|
Endoplasmic reticulum aminopeptidase 1 Recombinant
Endoplasmic reticulum aminopeptidase 1 Antibody
|Also known as Endoplasmic reticulum aminopeptidase 1 (ARTS-1) (Adipocyte-derived leucine aminopeptidase) (A-LAP) (Aminopeptidase PILS) (Puromycin-insensitive leucyl-specific aminopeptidase) (PILS-AP). |
ARTS1: 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. Belongs to the peptidase M1 family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: EC 3.4.11.-; Membrane protein, integral; Protease
Cellular Component: cytoplasm; endoplasmic reticulum lumen; extracellular region; extracellular space; intracellular membrane-bound organelle; membrane; plasma membrane
Molecular Function: aminopeptidase activity; endopeptidase activity; interleukin-6 receptor binding; metalloexopeptidase activity; peptidase activity; peptide binding; tumor necrosis factor receptor binding; zinc ion binding
Biological Process: antigen processing and presentation; antigen processing and presentation of endogenous peptide antigen via MHC class I; membrane protein ectodomain proteolysis; peptide catabolic process; positive regulation of angiogenesis; proteolysis; regulation of blood pressure
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