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Goat Anti-ERAP2 Antibody

Peptide-affinity purified goat antibody

     
  • WB - Goat Anti-ERAP2 Antibody AF1375a
    AF1375a (0.5 µg/ml) staining of Spleen lysate (35 µg protein in RIPA buffer). Primary incubation was 1 hour. Detected by chemiluminescence.
    detail
  • SPECIFICATION
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, E
Primary Accession Q6P179
Other Accession NP_071745, 64167
Reactivity Human
Predicted Dog, Cow
Host Goat
Clonality Polyclonal
Concentration 100ug/200ul
Isotype IgG
Calculated MW 110462 Da
Additional Information
Gene ID 64167
Other Names Endoplasmic reticulum aminopeptidase 2, 3.4.11.-, Leukocyte-derived arginine aminopeptidase, L-RAP, ERAP2, LRAP
Format 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsGoat Anti-ERAP2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ERAP2
Synonyms LRAP
Function 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. Preferentially hydrolyzes the basic residues Arg and Lys.
Cellular Location Endoplasmic reticulum membrane; Single-pass type II membrane protein
Tissue Location Ubiquitously expressed. Highly expressed in spleen and leukocytes.
Research Areas
Citations (0)
citation

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Background

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 [PubMed 12799365]).

References

Serum cytokine receptors in ankylosing spondylitis: relationship to inflammatory markers and endoplasmic reticulum aminopeptidase polymorphisms. Haroon N, et al. J Rheumatol, 2010 Sep. PMID 20595269.
Distinct molecular mechanisms leading to deficient expression of ER-resident aminopeptidases in melanoma. Kamphausen E, et al. Cancer Immunol Immunother, 2010 Aug. PMID 20419298.
NF-kappaB, and not MYCN, regulates MHC class I and endoplasmic reticulum aminopeptidases in human neuroblastoma cells. Forloni M, et al. Cancer Res, 2010 Feb 1. PMID 20103633.
The ERAP2 gene is associated with preeclampsia in Australian and Norwegian populations. Johnson MP, et al. Hum Genet, 2009 Nov. PMID 19578876.
Association of an ERAP1 ERAP2 haplotype with familial ankylosing spondylitis. Tsui FW, et al. Ann Rheum Dis, 2010 Apr. PMID 19433412.

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Discontinued
Cat# AF1375a
Size:
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