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ERAP2 Protein, Human, Recombinant (His)

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ERAP2 Protein, Human, Recombinant (His)

Catalog No. TMPY-00992

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.

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Pack Size	Price	Availability	Quantity
50 μg	$600	7-10 days

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Biological Description

Biological Information	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.
Description	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.
Species	Human
Expression System	HEK293 Cells
Tag	N-His
Accession Number	Q6P179-1
Synonyms	L-RAP,endoplasmic reticulum aminopeptidase 2,FLJ23633,LRAP.ERAP2,LRAP,FLJ23807,FLJ23701
Construction	lumenal domain of Human ERAP2 (NP_071745.1) (Ala 56-Thr 960)
Protein Purity	> 95 % as determined by SDS-PAGE
Molecular Weight	106 kDa (predicted)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Supplied as sterile 12. 5 mM Tris, 75 mM NaCl, pH 7.5, 50% glycercol.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store the product under sterile conditions at -20°C to -80°C. Samples are stable for up to 12 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry 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.