Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | B1AVD1 |
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 72.24 kDa. Due to glycosylation, the protein migrates to 75-105 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Mouse XPNPEP2 Protein 2721
$345.00 – $1,150.00
Summary
- Expression: HEK293
- Active: Yes (catalytic)
- Amino Acid Range: Pro23-Ala650
Mouse XPNPEP2 Protein 2721
protein |
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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 |
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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 76434Da |
Function 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. {ECO:0000250|UniProtKB:Q95333}. |
Catalytic activity CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000250|UniProtKB:Q95333}; |
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}. |
Tissues TISSUE SPECIFICITY: Strongly expressed in small intestine, heart and lung. Also detected in testis, skeletal muscle, spleen, liver, kidney, brain, uterus, eye, lymph node, thymus, stomach, prostate and bone marrow. {ECO:0000269|PubMed:12941294}. |
Structure SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q95333}. |
Post-translational modification PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99MA2}. |
Target Relevance information above includes information from UniProt accession: B1AVD1 |
The UniProt Consortium |
Data
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