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Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Additionally we are shipping Endoplasmic Reticulum Aminopeptidase 2 Antibodies (26) and Endoplasmic Reticulum Aminopeptidase 2 Kits (5) and many more products for this protein.
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Human ERAP2 Protein expressed in Human Cells - ABIN2003323
Tanioka, Hattori, Masuda, Nomura, Nakayama, Mizutani, Tsujimoto: Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. in The Journal of biological chemistry 2003
Show all 3 references for ABIN2003323
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.
Studies indicate the critical role of M1 aminopeptidases ERAP1 (show ERAP1 Proteins), ERAP2 and NPEPPS (show NPEPPS Proteins) in immune-mediated diseases.
The risk allele of the polymorphism near ERAP2 is strongly associated with birdshot chorioretinopathy.
Data indicate that dimerization of endoplasmic reticulum aminopeptidases ERAP1 (show ERAP1 Proteins)/2 creates complexes with superior peptide-trimming efficacy.
concerted aminoproteolytic activity of ERAP 1 (show ERAP1 Proteins) and ERAP2
ERAP2 haplotype A is correlated with resistance to HIV-1 infection, possibly secondarily to its effect on antigen processing and presentation.
ERAP1 (show ERAP1 Proteins) and ERAP2 might be involved in the development of immune escape mechanisms of renal cell carcinoma (show MOK Proteins).
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
endoplasmic reticulum aminopeptidase 2
, leukocyte-derived arginine aminopeptidase
, endoplasmic reticulum aminopeptidase 2-like