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Reconstitute at 0.2 mg/mL in sterile PBS.
The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) is a 120 kDa protein localized to the lumen of the ER, which removes NH2-terminal residues from many antigenic precursors for MHC class I peptide presentation. Peptides that are presented by MHC class I on the surface of a cell must be 8-11 residues long, and ERAP1 specifically trims peptides of 9 amino acids or more. ERAP1 is also induced by interferon- gamma. The gene encoding human ERAP1 maps to chromosome 5q15. ERAP1 has previously been characterized as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1). A-LAP is thought to inactivate several bioactive peptides, including angiotensin II and, subsequently, may be involved in the regulation of blood pressure. PILS-AP is described as playing a role in angiogenesis by regulating the proliferation and migration of endothelial cells, and ARTS-1 is characterized as a TNFR1 binding protein that promotes TNFR1 shedding. Further research will be necessary to fully elucidate the functions of this protein.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: A-LAP; Adipocyte-derived leucine aminopeptidase; Aminopeptidase PILS; ARTS-1; Endoplasmic reticulum aminopeptidase 1; PILS-AP; Puromycin-insensitive leucyl-specific aminopeptidase; type 1 tumor necrosis factor receptor shedding aminopeptidase regulator; VEGF-induced aminopeptidase
基因别名: Appils; Arts1; ERAAP; Erap1; PILSA; PILSAP
UniProt ID: (Mouse) Q9EQH2
Entrez Gene ID: (Mouse) 80898