|Other Names||Endoplasmic reticulum aminopeptidase 2, 3411-, Leukocyte-derived arginine aminopeptidase, L-RAP, ERAP2, LRAP|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. 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.
Aminopeptidases hydrolyze N-terminal amino acids ofproteins or peptide substrates. Major histocompatibility complex(MHC) class I molecules rely on aminopeptidases such as ERAP1 (MIM606832) and LRAP to trim precursors to antigenic peptides in theendoplasmic reticulum (ER) following cleavage in the cytoplasm bytripeptidyl peptidase II (TPP2; MIM 190470) (Tanioka et al., 2003[PubMed 12799365]).
Saveanu, L., et al. Nat. Immunol. 6(7):689-697(2005)Tanioka, T., et al. FEBS J. 272(4):916-928(2005)Tanioka, T., et al. J. Biol. Chem. 278(34):32275-32283(2003)Hattori, A., et al. J. Biochem. 130(2):235-241(2001)
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