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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 Proteins (7) and ERAP1 Kits (4) and many more products for this protein.
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Data demonstrate that HCMV miR (show MLXIP Antibodies)-UL112-5p targets ERAP1, thereby inhibiting the processing and presentation of the HCMV pp65495-503 peptide to specific CTLs.
these results present the first direct evidence that human disease-associated ERAP1 variants can greatly alter survival, as well as antigen presentation, T-cell repertoire and NK cell responses in vivo in mice
The ERAP1 association with ankylosing spondylitis is predominantly attributable to common ERAP1 haplotypes and haplotype combinations.
these study reports an association of the ERAP1 SNP rs30187 with the HLA-C*07 allele in inflammatory bowel disease in the Spanish population
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 (show MRAP Antibodies) in autoimmunity and viral protection correlating its functions to the quantitative and qualitative effects of ERAP1 and ERAP2 (show ERAP2 Antibodies) 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 Antibodies) 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 (show MRAP Antibodies) in monocytes, and thus help to maintain the integrity of cell surface HLA-B27 (show MRAP Antibodies) complexes.
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 Antibodies)) forms a mixed disulfide bond with aminopeptidase (show ANPEP Antibodies) 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 Antibodies)-like receptors via induction of intermediate cytokines
ERAP1 directly alters peptide binding and presentation by HLA-B27 (show MRAP Antibodies), 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 Antibodies)
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