Recombinant Human LRAP/ERAP2 Protein (His Tag)(Active) | PKSH031454

Recombinant Human LRAP/ERAP2 Protein (His Tag)(Active) | PKSH031454 | Gentaur US, UK & Europe Disrtribition

Synonyms: FLJ23633;FLJ23701;FLJ23807;L-RAP;LRAP;LRAP.ERAP2

Active Protein: Active protein

Activity: 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.

Protein Construction: 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.

Fusion Tag: N-His

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 98 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 106 kDa

Formulation: Lyophilized from sterile 12.5mM Tris, 75mM NaCl, pH 7.5, 50% glycercol

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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.

Research Area: Cell biology, immunology