ERAP2 Protein, Human, Recombinant (His)

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 96-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.

Pack Size	Availability	Price/USD	Quantity
50 μg	5 days	$ 600.00

Pack Size

Availability

Price/USD

Quantity

50 μg

5 days

$ 600.00

Description

Species	Human
Expression System	HEK293
Tag	His
Accession Number	Q6P179-1
Synonyms	L-RAP, endoplasmic reticulum aminopeptidase 2, FLJ23633, LRAP.ERAP2, LRAP, FLJ23807, FLJ23701
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.
Protein Purity	> 95 % as determined by SDS-PAGE
Molecular Weight	106 kDa (predicted)

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Supplied as sterile 12. 5mM Tris, 75mM NaCl, pH 7.5, 50% glycercolPlease contact us for any concerns or special requirements. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping	Solution. It is shipped out with blue ice.
Research 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 96-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.