Recombinant Human Aminopeptidase P2/XPNPEP2 Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 2490-ZN
Key Product Details
Product Specifications
Source
Mouse myeloma cell line, NS0-derived human Aminopeptidase P2/XPNPEP2 protein
His22-Ala650, with a C-terminal 10-His tag
His22-Ala650, with a C-terminal 10-His tag
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
His22 & Lys24
Predicted Molecular Mass
72 kDa
SDS-PAGE
85 kDa, reducing conditions
Activity
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, as measured under the described conditions.
The specific activity is >300 pmol/min/µg, as measured under the described conditions.
Formulation, Preparation and Storage
2490-ZN
| Formulation | Supplied as a 0.2 μm filtered solution in Tris and NaCl. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Aminopeptidase P2/XPNPEP2
The human XPNPEP2 gene encodes Aminopeptidase P2 (APP2), which is also known as X-prolyl Aminopeptidase 2 or membrane bound Aminopeptidase P (1‑4). It is a member of the M24 family of metalloproteases, which also contains methionine Aminopeptidases, X-Pro dipeptidase, Aminopeptidase P1, Aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit (5). Mammalian APP2 are predicted to be GPI-anchored membrane proteases and their biological functions have been reviewed (6). Human APP2 is widely expressed in many adult tissues with the highest levels in the kidney (7). The purified recombinant human APP2 corresponds to the ectodomain and is shown here to be an active aminopeptidase, removing a N-terminal amino acid from a peptide that contains a Pro residue at the second position.
References
- Venema, R.C. et al. (1997) Biochim. Biophys. Acta 1354:45.
- Sprinkle, T.J. et al. (1998) Genomics 50:114.
- Cottrell, G.S. et al. (1998) Biochem. Soc. Trans. 26:S248.
- Prueitt, R.L. et al. (2000) Cytogenet. Cell Genet. 89:44.
- Barrett, A.J. et al. (2004) Handbook of Proteolytic Enzymes, Elsevier Academic Press, San Diego.
- Simmons, W.H. (2004) in Handbook of Proteolytic Enzymes (Barrett, A.J. et al. eds.) p. 934, Elsevier Academic Press, San Diego.
- Ersahin C. et al. (2005) Arch. Biochem. Biophys. 435:303.
Alternate Names
XPNPEP2
Gene Symbol
XPNPEP2
UniProt
Additional Aminopeptidase P2/XPNPEP2 Products
Product Documents for Recombinant Human Aminopeptidase P2/XPNPEP2 Protein, CF
Product Specific Notices for Recombinant Human Aminopeptidase P2/XPNPEP2 Protein, CF
The purchase of this product conveys to the buyer the limited, non-exclusive, non-transferable right (without the right to resell, repackage, or further sublicense) to use these reagents for non-commercial research purposes only. No other license is granted to the buyer whether expressly, by implication, by estoppel or otherwise. In particular, the purchase of this product does not include nor carry any right or license to use, develop, or otherwise exploit this product commercially, which includes without limitation, provision of services to a third party, generation of commercial databases, clinical diagnostics or therapeutics, or drug development. This Product is manufactured under a license to U.S. Patent Nos. 6,399,349 and 7,273,718.
Any party desiring rights under this patent should contact Ryogen LLC, Montebello Park, 75 Montebello Road, Suffern, NY 10901.
For research use only
Loading...
Loading...
Loading...