The Recombinant Human ERAP2 Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating ERAP2 function and its implications in health and disease.
This product (SKU: RPCB1946) is produced using HEK293 cells and features a N-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 115-125 kDa. with an observed molecular weight of - under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE.. Functional bioactivity has been validated through rigorous quality control assays, confirming its suitability for demanding research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human ERAP2 Protein (RP03147LQ), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 1 EU/μg of the protein by LAL method.
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Supplied as a 0.22 μm filtered solution in 12.5mM Tris, 75mM NaCl, pH 7.5, 50% glycercol. Contact us for customized product form or formulation.
Bio-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.
Storage:
Store at -70℃. This product is stable at ≤ -70℃ for up to 1 year from the date of receipt. For optimal storage, aliquot into smaller quantities after centrifugation and store at recommended temperature. Avoid repeated freeze-thaw cycles.
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.
Recombinant Human ERAP2 Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
