Human ERAP2 (His Tag) recombinant protein

Human ERAP2 (His Tag) recombinant protein

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Leukocyte-derived arginine aminopeptidase (LRAP), also known as endoplasmic reticulum-aminopeptidase 2 (ERAP2), is the second identified aminopeptidase localized in the in the lumenal side of endoplasmic reticulum (ER) processing antigenic peptides presented to major histocompatibility complex (MHC) class I molecules. It is a 960-amino acid protein with significant homology to placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase. LRAP preferentially hydrolyzes the basic residues Arg and Lys, and contains the HEXXH(X)18E zinc-binding motif, which is the characteristic of the M1 family of zinc metallopeptidases which also includes PILS/ARTS1/ERAP1 and LNPEP/PLAP. Induced by interferon-gamma, LRAP is able to trim various MHC class I antigenic peptide precursors.

cDNA, FLJ93308, highly similar to Homo sapiens leukocyte-derived arginine aminopeptidase (LRAP)

LRAP; FLJ23807; ERAP2; FLJ23633; L-RAP; FLJ23701

Q6P179

Human Cells

A DNA sequence encoding the lumenal domain of human ERAP2 (NP_071745.1) (Ala 56-Thr 960) was expressed with a polyhistidine tag at the N-terminus.

Human

The recombinant human ERAP2 consists of 921 amino acids and predictes a molecular mass of 106 kDa. In SDS-PAGE under reducing conditions, it migrates with the apparent molecular mass of 115-125 kDa due to glycosylation.

> 98 % as determined by SDS-PAGE

Measured by its ability to cleave the fluorogenic peptide substrate, Arg-7-amido-4-methylcoumarin (Arg-AMC). The specific activity is >50 pmoles/min/μg.