Human NTPDase 2 / ENTPD2 Protein (aa 29-460, His Tag)
CD39L1,NTPDase-2
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Catalog Number | P11734-H07B1 |
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Organism Species | Human |
Host | Baculovirus-Insect Cells |
Synonyms | CD39L1,NTPDase-2 |
Molecular Weight | 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. |
predicted N | His |
SDS-PAGE | |
Purity | > 85 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the mature form of human ENTPD2 (Q9Y5L3) (Thr29-Asp460) was expressed, with a polyhistidine tag at the N-terminus. |
Bio-activity | Measured by its ability to hydrolyze the 5’phosphate groups from the substrate adenosine 5’triphosphate(ATP). The specific activity is > 5,000 pmoles/min/μg. |
Research Area | Signaling |Signal Transduction |Metabolism |Types of disease |Metabolism in Cancer |
Formulation | Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
Background | NTPDase 2, also known as ENTPD2, belongs to the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). Members of E-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. NTPase activity would act as a timer and is crucial to T. gondii infection. In L. pneumophila it was demonstrated that an E-NTPDase, similar to CD39, is essential for intracellular bacterial multiplication. NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Alternative splicing of NTPDase 2 gene results in multiple transcript variants. |
Reference |