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The protein encoded by ERAP1 is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. Additionally we are shipping ERAP1 Antibodies (69) and ERAP1 Kits (4) and many more products for this protein.
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Study suggests that ERAP1 rs27044 polymorphism may be related to ankylosing spondylitis susceptibility in Chinese Han population.
Segregating according to HLAB27 status did not alter the lack of association. rs30187 SNP in ERAP1 does not confer risk of developing ERA or AS in the Asian Indian population.
ERAP1 and ERAP2 have significant and distinct effects on the HLA-B*27 peptidome, suggesting that both enzymes largely act as separate entities in vivo. This may explain their different patterns of association with AS.
This review focuses on the ambivalent role of HLA-B27 in autoimmunity and viral protection correlating its functions to the quantitative and qualitative effects of ERAP1 and ERAP2 (show ERAP2 Proteins) polymorphisms on their enzymatic activity.
The ERAP1 gene polymorphism might be a risk factor in the pathogenesis of ankylosing spondylitis and inflammatory bowel disease. In contrast, IL-23R (show IL23R Proteins) gene polymorphisms may serve a protective role in ankylosing spondylitis and inflammatory bowel disease.
Our results suggest that normal levels of ERAP1 reduce the accumulation of aberrant and disulfide-linked forms of HLA-B27 in monocytes, and thus help to maintain the integrity of cell surface HLA-B27 complexes.
The alterations in the nature and affinity of HLA-B*51.peptide complexes probably affect T-cell and natural killer cell recognition, providing a sound basis for the joint association of ERAP1 and HLA-B*51 with Behcet's disease.
One ERAP1 protein allotype with five non-ancestral amino acids was recessively associated with Behcet's disease. The ERAP1 association was absent in individuals who lacked HLA-B*51. Individuals who carry HLA-B*51 and who are also homozygous for the haplotype had an increased disease odds compared with those with neither risk factor.
Electrostatic interactions between domains II and IV in ERAP1 are crucial for driving a conformational change that regulates the structural integrity of the catalytic site.
analysis of genotype and haplotype frequencies of four coding, nonsynonymous ERAP1 SNPs, rs26653G > C, rs26618T > C, rs30187C > T, and rs27044C > G, in non-small cell lung carcinoma occurring in two genetically distant populations, Chinese and Poles
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
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
Data show that endoplasmic reticulum protein 44 (ERp44 (show ERP44 Proteins)) forms a mixed disulfide bond with aminopeptidase (show ANPEP Proteins) ERAP1 and controls the release of ERAP1 in a redox-dependent manner to control blood pressure.
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.
These results suggest that secretion of ERAP1 is mediated by toll (show TLR4 Proteins)-like receptors via induction of intermediate cytokines
ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis.
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.
MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo.
endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma (show IFNG Proteins)
ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice
The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.
endoplasmic reticulum aminopeptidase 1
, endoplasmic reticulum aminopeptidase 1-like
, type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
, adipocyte-derived leucine aminopeptidase
, aminopeptidase PILS
, aminopeptidase regulator of TNFR1 shedding
, endoplasmic reticulum aminopeptidase associated with antigen processing
, puromycin-insensitive leucyl-specific aminopeptidase
, VEGF-induced aminopeptidase
, ER-aminopeptidase 1
, leucyl-specific aminopeptidase PILS