Name :
Recombinant Human ERAP2 Protein (His Tag)
Biological Activity :
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.
Biological Activity :
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.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_071745.1
NCBI Gene ID :
Synonyms :
Synonyms :
endoplasmic reticulum aminopeptidase 2
Amino Acid Sequence :
Molecular Weight :
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.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
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.
Buffer Solution :
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 hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
FLJ23633 Protein, Human; FLJ23701 Protein, Human; FLJ23807 Protein, Human; L-RAP Protein, Human; LRAP Protein, Human; LRAP.ERAP2 Protein, Human ERAP2 背景信息 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.
References & Citations :
Tanioka T., et al.,(2003), Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J. Biol. Chem. 278:32275-32283.Tanioka T., et al., (2005), Regulation of the human leukocyte-derived arginine aminopeptidase/endoplasmic reticulum-aminopeptidase 2 gene by interferon-gamma.FEBS J. 272:916-928.Liu T., et al.,(2005), Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.J. Proteome Res. 4:2070-2080.
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