Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
accession | Q99MA2 |
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 72.05 kDa. Due to glycosylation, the protein migrates to 75-85 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Rat XPNPEP2 Protein 2891
$345.00 – $1,150.00
Summary
- Expression: HEK293
- Active: Yes (catalytic)
- Amino Acid Range: Pro23-Ala650
Rat XPNPEP2 Protein 2891
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) (Membrane-bound aminopeptidase P) (Membrane-bound APP) (mAPP) (X-prolyl aminopeptidase 2) |
Gene names Xpnpep2,Xpnpep2 |
Protein family Peptidase M24B family |
Mass 10116Da |
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 strongly in lung, liver and heart, and at lower levels in kidney, testis, brain, spleen and skeletal muscle. |
Structure Homotrimer. |
Post-translational modification N-glycosylated. |
Target Relevance information above includes information from UniProt accession: Q99MA2 |
The UniProt Consortium |
Publications
pmid | title | authors | citation |
---|---|---|---|
We haven't added any publications to our database yet. |
relevant to this product |
---|
# | ||
---|---|---|
Please enter your product and batch number here to retrieve product datasheet, SDS, and QC information. |