Erap1 Antibody

Code CSB-PA007760ZA01MO
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Product Details

Full Product Name
Rabbit anti-Mus musculus (Mouse) Erap1 Polyclonal antibody
Uniprot No.
Target Names
Alternative Names
Erap1 antibody; Appils antibody; Arts1Endoplasmic reticulum aminopeptidase 1 antibody; EC 3.4.11.- antibody; ARTS-1 antibody; Adipocyte-derived leucine aminopeptidase antibody; A-LAP antibody; Aminopeptidase PILS antibody; Puromycin-insensitive leucyl-specific aminopeptidase antibody; PILS-AP antibody; VEGF-induced aminopeptidase antibody
Raised in
Species Reactivity
Mus musculus
Recombinant Mus musculus Erap1 protein
Immunogen Species
Mus musculus (Mouse)
Purification Method
Protein A/G
It differs from different batches. Please contact us to confirm it.
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Tested Applications
ELISA, WB (ensure identification of antigen)
Troubleshooting and FAQs
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (12-14 weeks)

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Target Background

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.
Gene References into Functions
  1. data provide the first evidence that ERAP1 associated with exosomes plays important roles in inflammatory processes via activation of macrophages. PMID: 29567213
  2. we have shown that the loss of ERAAP leads to shifts in the nature and lengths of peptides presented by MHC I molecules on the cell surface PMID: 27371725
  3. results suggest that several aminopeptidases play important roles in the maximum synthesis of NO in activated macrophages in a substrate peptide-dependent manner and ERAP1 is one of the aminopeptidases involved in the NO synthesis PMID: 25577645
  4. This study clarifies ERAP1's role in shaping immunodominance through creation and destruction of peptides in vivo and demonstrates the functional significance of ERAP1 in modulating T-cell killing based upon this role. PMID: 25087231
  5. These results suggest that secretion of ERAP1 is mediated by toll-like receptors via induction of intermediate cytokines PMID: 24688025
  6. ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis. PMID: 24504800
  7. Absence of Tpn or ERAAP independently altered the peptide repertoire by causing loss as well as gain of new pMHC I. ERAAP defined the characteristic amino termini of canonical MHC I peptides. PMID: 23863903
  8. MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo. PMID: 22522492
  9. endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma PMID: 21531727
  10. ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice PMID: 21252114
  11. The characteristic peptide length, as well as composition, of class I histocompatibility peptide cargo is determined not only by the class-I peptide-binding groove, but also by ERAAP proteolysis in the endoplasmic reticulum. PMID: 20173027
  12. identification of ERAAP, the aminopeptidase associated with antigen processing in the endoplasmic reticulum (ERAAP) PMID: 12368856
  13. Data show that loss of endoplasmic reticulum aminopeptidase 1 (ERAP1) in the antigen-processing pathway results in a marked shift in the hierarchy of immunodominance in viral infections. PMID: 16754858
  14. Although PILSAP may not function in the initial generation of Flk-1 positive mesodermal precursors, it does play a role in growth of vascular, hematopoietic, and muscular lineage population from those precursors. PMID: 16824192
  15. PILSAP affects RhoA activation and that influences the proper function of endothelial cells PMID: 17385722
  16. ERAAP, in concert with major histocompatibility complex class I molecules, regulates the quality of processed peptides presented on the cell surface. PMID: 18941218

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Subcellular Location
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Protein Families
Peptidase M1 family
Database Links
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