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Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Additionally we are shipping Endoplasmic Reticulum Aminopeptidase 2 Antibodies (27) and Endoplasmic Reticulum Aminopeptidase 2 Kits (7) and many more products for this protein.
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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 (show ERAP1 Proteins) and ERAP2 polymorphisms on their enzymatic activity.
ERAP2 deficiency causes increased MHC class I free heavy chain expression and up-regulation of the unfolded protein response pathway in anklyosing spondylitis.
ERAP-2 significantly influences the B*27:05-bound peptidome by destroying some ligands and decreasing the abundance of many more ligands with N-terminal basic residues, while increasing the abundance of nonamers. The former effects are best explained by direct ERAP-2 trimming. The effects on peptide length might be attributed to ERAP-2-induced activation of ERAP-1 (show ERAP1 Proteins) trimming. These data support the notion of a peptide-media
study reveals fine-mapped AID risk variants that act as eQTLs with ERAP2 in thymus
there is a significant association of ERAP2 with psoriatic arthritis and HLA-B27 negative psoriatic arthritis, while ERAP1 association is restricted only to HLA-B27 positive disease
Increased expression of ERAP2 in GC-responders before therapy warrants further investigation into their role as potential predictors for the response to GC, and in the inflammatory process of rheumatoid arthritis.
ERAP2 is associated with ankylosing spondylitis in HLA-B27 positive and HLA-B27 negative patients.
ERAP2 might be associated with CLNM in PTMC.
ERAP2 variation does not have a significant effect on PBMC intracellular and cell surface HLA-class I (show MICA Proteins) expression and heavy chain formation, markers of ER stress or inflammatory cytokine production.
Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 (MIM 606832) and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2\; MIM 190470) (Tanioka et al., 2003
leukocyte-derived arginine aminopeptidase
, endoplasmic reticulum aminopeptidase 2
, endoplasmic reticulum aminopeptidase 2-like