Human XPNPEP2 Protein 2718

$345.00 – $1,150.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: His22-Ala649

SKU: 2718parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	O43895
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Aminopeptidase P2 (XPNPEP2) is a receptor for TMTP1 tumor-homing peptide. However, the biological and clinical significance of Aminopeptidase P2 in human cancers remains unknown.
molecular weight	The protein has a predicted MW of 71.83 kDa. Due to glycosylation, the protein migrates to 73-83 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human XPNPEP2 Protein 2718

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Aminopeptidase P2 (XPNPEP2) is a receptor for TMTP1 tumor-homing peptide. However, the biological and clinical significance of Aminopeptidase P2 in human cancers remains unknown.
Protein names Xaa-Pro aminopeptidase 2 (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Membrane-bound aminopeptidase P) (Membrane-bound APP) (Membrane-bound AmP) (mAmP) (X-Pro aminopeptidase 2)
Gene names XPNPEP2,XPNPEP2
Protein family Peptidase M24B family
Mass 9606Da
Function Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin.
Catalytic activity BINDING 116; /ligand="substrate"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 430; /ligand="substrate"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 450; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 461; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 461; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 524; /ligand="substrate"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 524; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 533; /ligand="substrate"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 555; /ligand="substrate"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 555; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 569; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000250\|UniProtKB:O44750"; BINDING 569; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000250\|UniProtKB:O44750"
Subellular location Cell membrane ; Lipid-anchor, GPI-anchor .
Tissues Expressed in kidney, lung, heart, placenta, liver, small intestine and colon. No expression in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary.
Structure Homotrimer.
Post-translational modification N-glycosylated.
Target Relevance information above includes information from UniProt accession: O43895
The UniProt Consortium

Data

Activity assay with Human XPNPEP2 Protein

Measured by its ability to cleave the fluorogenic peptide substrate, H-Lys(2-Aminobenzoyl)-Pro-Pro-p-Nitroanilide (K(Abz)PP-pNA). The specific activity is > 300 pmol/min/µg.

The purity of Human XPNPEP2 is greater than 95% as determined by SEC-HPLC.

Human XPNPEP2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.