|Application ||WB, E|
|Other Accession||NP_071745, 11641261|
|Calculated MW||Predicted: 106 kDa |
|Application Notes||ERAP2 antibody can be used for detection of ERAP2 by Western blot at 1 - 2 µg/ml.|
|Target/Specificity||ERAP2; ERAP2 antibody is human reactive. Multiple isoforms of ERAP2 are known to exist. ERAP2 antibody is predicted to not cross-react with ERAP1.|
|Reconstitution & Storage||ERAP2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||ERAP2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
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Provided below are standard protocols that you may find useful for product applications.
The endoplasmic reticulum (ER) aminopeptidase 2 (ERAP2), a member of the peptidase M1 family, like the related protein ERAP1, plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides (1,2). Like ERAP1, ERAP2 is localized to the lumen of the ER and is thought to associate with ERAP1 as a heterodimer (1). Both ERAP1 and ERAP2 have been linked to several human diseases ranging from infections to autoimmunity and cancer, and may play a role in the innate immune response (reviewed in 3).
Saveanu L, Carroll O, Lindo V, et al. Concerted peptide trimming by EARP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat. Immunol. 2005; 6:689-97.
Saric T, Chang SC, Hattori A, et al. An IFN-gamma induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 2002; 3:1169-76.
Cifaldi L, Romania P, Lorenzi S, et al. Role of endoplasmic reticulum aminopeptidases in health and disease: from infection to cancer. Int. J. Mol. Sci. 2012; 13:8338-52
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