NTPDase 2 / ENTPD2 (aa 29-460) Protein (His Tag)

Produkt-Information von NTPDase 2 / ENTPD2 Protein

QC Testing von NTPDase 2 / ENTPD2 Protein

Purity	> 85 % as determined by SDS-PAGE	SDS-PAGE: NTPDase 2 / ENTPD2 protein
Bio-activity	Measured by its ability to hydrolyze the 5’phosphategroups from the substrate adenosine 5’triphosphate(ATP). The specific activity is > 5,000 pmoles/min/μg.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	His
Molecular Mass	The recombinant human human ENTPD2 consists of  448 amino acids and predicts a molecular mass of 49.3 KDa. It migrates as an approximately 59 KDa band in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from a 0.2μm filtered solution of 20mM Tris, 500mM NaCl, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von NTPDase 2 / ENTPD2 Protein

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Enzyme >>Other>> NTPDase 2 / ENTPD2

Beschreibung von NTPDase 2 / ENTPD2 Protein

NTPDase 2, also known as ENTPD2, is the type 2 enzyme of the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). E-NTPDases are a family of ecto-nucleosidases that hydrolyze 5'-triphosphates. Members of Ecto-NTPDase family are nucleotidases able to hydrolyze 5′-nucleoside tri- and/or diphosphates; the main role of these enzymes is the termination of purinergic signaling. NTPDases are ubiquitous and were previously shown in other parasites including the trypanosomatides of genus Leishmania and in T. brucei . NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. NTPDase 2 stimulates the growth of the eye: by testing the enzyme on tadpoles, the tadpoles were found to develope extra eyes on their body.

References

1. Harden TK. et al., 2005, Mol Pharmacol. 67 (1): 114-22.
2. Dranoff JA. et al., 2005, J Investig Med. 52 (7): 475-82.
3. Jhandier MN. et al., 2005, J Biol Chem. 280 (24): 22986-92.
4. Mukasa T. et al., 2005, Biochemistry. 44 (33): 11160-70.

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