Specification
| Description | Recombinant protein from the full-length sequence of Homo sapiens nudix hydrolase 15 (NUDT15), transcript variant 1 (NM_018283). |
| Organism | Homo sapiens (Human) |
| Expression Host | Human Cells |
| Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
| Purity | Greater than 90% by SDS-PAGE gel |
| Uniprot ID | Q9NV35 |
| Entry Name | NUD15_HUMAN |
| Gene Names | NUDT15 MTH2 |
| Alternative Gene Names | MTH2 |
| Alternative Protein Names | Nucleotide triphosphate diphosphatase NUDT15 (EC 3.6.1.9) (MutT homolog 2) (MTH2) (Nucleoside diphosphate-linked moiety X motif 15) (Nudix motif 15) (Nucleoside diphosphate-linked to another moiety X hydrolase 15) (Nudix hydrolase 15) |
| Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
| Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
| Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
| Length | 164 |
| Molecular Weight(Da) | 18609 |
| Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MTASAQPRGRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEECAQRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSEPKNVEPEKNESWEWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVGYKGNHL |
Background
| Function | FUNCTION: May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP (PubMed:26238318). Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives (PubMed:22556419, PubMed:26238318). Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear (PubMed:26238318, PubMed:22556419). Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs (PubMed:26238318, PubMed:25108385). May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA (PubMed:19419956). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:Q8BG93, ECO:0000269|PubMed:19419956, ECO:0000269|PubMed:22556419, ECO:0000269|PubMed:25108385, ECO:0000269|PubMed:26238318}. |
| Pathway | |
| Protein Families | Nudix hydrolase family |
| Tissue Specificity |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |