|Application ||WB, E|
|Other Accession||P0C028, Q96G61, Q58CW0, P0C027, NP_694853.1|
|Calculated MW||18500 Da|
|Antigen Region||1-30 aa|
|Other Names||Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5', 5'''-P1, P6-hexaphosphate hydrolase 3-alpha, Diadenosine hexaphosphate hydrolase (AMP-forming), Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A|
|Target/Specificity||This NUDT10 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human NUDT10.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NUDT10 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.|
|Tissue Location||Mainly expressed in testis and, at lower level in brain. According to PubMed:12121577, it is widely expressed|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
NUDT10 belongs to a subgroup of phosphohydrolases that preferentially attack diphosphoinositol polyphosphates (Hidaka et al., 2002 [PubMed 12105228]).
Kim, S.T., et al. Prostate 70(16):1729-1738(2010)
Gudmundsson, J., et al. Nat. Genet. 40(3):281-283(2008)
Eeles, R.A., et al. Nat. Genet. 40(3):316-321(2008)
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Ross, M.T., et al. Nature 434(7031):325-337(2005)
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