Recombinant Human 7,8-Dihydro-8-Oxoguanine Triphosphatase (NUDT1)

Name: Recombinant Human 7,8-Dihydro-8-Oxoguanine Triphosphatase (NUDT1)
Brand: Beta LifeScience
SKU: BLC-09246P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human 7,8-Dihydro-8-Oxoguanine Triphosphatase (NUDT1) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P36639
Target Symbol	NUDT1
Synonyms	2-hydroxy-dATP diphosphatase; 7 8 dihydro 8 oxoguanine triphosphatase; 7; 8 oxo 7 8 dihydrodeoxyguanosine triphosphatase; 8 oxo 7 8 dihydroguanosine triphosphatase; 8 oxo dGTPase; 8-dihydro-8-oxoguanine triphosphatase; 8-oxo-dGTPase; 8ODP_HUMAN; MTH 1; MTH1; MutT human homolog 1; Nucleoside diphosphate linked moiety X motif 1; Nucleoside diphosphate linked moiety X type motif 1; Nucleoside diphosphate-linked moiety X motif 1; Nudix (nucleoside diphosphate linked moiety X) type motif 1; Nudix hydrolase 1; Nudix motif 1; Nudix type motif 1; NUDT 1; Nudt1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MSGISPQQMGEPEGSWSGKNPGTMGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV
Expression Range	19-197aa
Protein Length	Full Length of Mature Protein
Mol. Weight	20.3 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress.
Subcellular Location	[Isoform p18]: Cytoplasm, cytosol. Mitochondrion matrix. Nucleus.; [Isoform p26]: Mitochondrion matrix.
Protein Families	Nudix hydrolase family
Database References	HGNC: 8048 OMIM: 600312 KEGG: hsa:4521 STRING: 9606.ENSP00000339503 UniGene: PMID: 29661172 MTH1 is required for maintaining migration and invasion potential of human thyroid cancer cells. PMID: 30055508 PRDX1 and MTH1 cooperate to prevent accumulation of oxidized guanine in the genome PMID: 29773556 Results provide evidence that MTH1 is not essential for cancer cell survival. PMID: 27210421 CDT1, MCM7, and NUDT1 were shown to be up-regulated in hepatocellular carcinoma tissues and provide a more accurate diagnosis than alpha-fetal protein alone. PMID: 29442275 Our results reveal a novel antitumor mechanism of (S)-crizotinib in NSCLC which involves activation of ROS-dependent ER stress apoptotic pathway and is independent of MTH1 inhibition PMID: 28882182 this study showed that MTH1 protein expression was closely related to factors associated with a high malignant potential and poor patient survival PMID: 28577950 method for predicting individual residue contributions to enzyme specificity and binding-site energies, and its application to MTH1. PMID: 27714533 Data indicate the specificity of the enzyme 8-oxo-dGTPase MTH1 toward the substrate 8-oxo-dGTP. PMID: 27350386 We demonstrate that in order to kill cancer cells MTH1 inhibitors must also introduce oxidized nucleotides into DNA. Furthermore, we describe TH1579 as a best-in-class MTH1 inhibitor, which we expect to be useful in order to further validate the MTH1 inhibitor concept. PMID: 27827301 Data indicate a positive correlation of Skp2 and MTH1 expression in melanoma cell lines and patient specimens. PMID: 28947420 Results show that MTH1 is overexpressed in esophageal squamous cell carcinoma, and suggestive of disease progression. PMID: 27917618 MTH1 together with MYH plays an important role in protection against mutations induced by modified dNTPs during chronic oxidative stress. PMID: 28340109 Reduced MUTYH, MTH1, and OGG1 expression and TP53 mutations occur in diffuse-type adenocarcinoma of gastric cardia. PMID: 26980051 Analyses of bond lengths with high-resolution X-ray data and the relationship between the structure and enzymatic activity revealed that hMTH1 recognizes the different oxidized nucleotides via an exchange of the protonation state at two neighboring aspartate residues (Asp-119 and Asp-120) in its substrate binding pocket PMID: 28035004 MTH1 inhibition may offer a general approach to treat cancers characterized by deregulated hypoxia signaling or redox imbalance PMID: 26862114 MTH-1 expression in colorectal cancer cells was upregulated via HIF-1alpha in response to hypoxic stress, emphasizing the crucial role of HIF-1alpha-induced MTH-1 in tumor growth. PMID: 26730155 activity of MTH1 in different breast cancer cell lines has been detected, implying the potential application of this assay method for biomedical research and clinical diagnose in the future PMID: 26755138 a novel approach involving liquid chromatography-isotope-dilution tandem mass spectrometry to positively identify and accurately quantify MTH1 in human tissues, is reported. PMID: 26202347 MTH1 is the most prominent sanitizer of the cellular dNTP pool known to date. PMID: 26238318 MTH1 expression is required for effective transformation of epithelial cells by oncogenic HRAS. PMID: 25893378 Results show that MTH1 plays no role in protecting the cells against ultraviolet radiation-induced cytogenetic damage. PMID: 26520386 Results suggest that the hMTH1-mediated maintenance of mtDNA stability protects cells from the susceptibility to oxidant injury associated with polyQ-expanded Htt, defends against 3-nitropropionic acid-induced neurodegeneration PMID: 22974734 results indicate MTH1 is a novel and critical component of oncogenic KRAS-associated malignancy and its inhibition is likely to yield significant tumor-suppressive outcomes in KRAS-driven tumors. PMID: 25023700 The ectopic expression of hMTH1 in the chloroplasts and mitochondria of Arabidopsis enhanced oxidative stress tolerance by activating the poly(ADP-ribosyl)ation (PAR)reaction and suppressing programmed cell death. PMID: 24928220 Data suggest that hOGG1 could compensate for hMTH1 during oxidative DNA damage caused by H2O2, whereas hMTH1 could not compensate sufficiently for hOGG1 during the process. PMID: 25127756 cancer cells require MTH1 activity to avoid incorporation of oxidized dNTPs, resulting in DNA damage and cell death; validation of MTH1 as an anticancer target in vivo PMID: 24695224 MTH1 protects cells from mutagenesis induced by ultraviolet ray A and B, but not ultraviolet ray C.hMTH1 prevents induction of transition-type mutations at AT and GC post ultraviolet ray A irradiation. PMID: 24144844 X-ray crystallographic analysis of MTH1 protein structure PMID: 23295485 The risk of type 2 diabetes in the Chinese population is increased from the combined effects of AluYb8MUTYH with either hMTH1 c.247G>A or variants in the 5\'-UTR of the hOGG1. PMID: 23396182 The study provides insight into the influence of MTH1 levels on the epithelial-mesenchymal transition phenotype and Akt activation in RAS-transformed HMLE breast epithelial cells. PMID: 22790201 MutT homolog-1 attenuates oxidative DNA damage and delays photoreceptor cell death in inherited retinal degeneration. PMID: 22841817 These results suggest that MTH1 deficiency might be a causative factor for aging and age-related disorders. PMID: 21538080 results indicate that the nucleotide pool is a significant target for UVA-induced mutations and implicates that hMTH1 plays an important role in protecting cells from UVA-induced oxidative stress PMID: 21784087 the structures of human MTH1 (1.9A) and its complex with the product 8-oxo-dGMP PMID: 21787772 Manipulation of miR-145 expression modulates epidermal growth factor receptor (EGFR) and NUDT1 mRNA expressions. PMID: 21289483 The expression levels of hMTH1 mRNA are highly correlated with hepatic levels of 8-oxo-dG and tail moment, suggesting that hMTH1 gene expression represents a molecular marker of oxidative DNA damage. PMID: 21421019 Two rare variants (OGG1 c.137G>A; MUTYH c.1187G>A) and one common polymorphism (NUDT1 c.426C>T) were associated with colorectal cancer risk. PMID: 21355073 human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP. PMID: 20144704 Trp-117 is essential for MTH1 to recognize both 8-oxo-dGTP and 2-hydroxy-dATP, whereas Asp-119 is only essential for recognizing 2-hydroxy-dATP, thus suggesting that origins of the substrate-binding pockets for MTH1 and MutT are different PMID: 11756418 8-Chloro-dGTP, a hypochlorous acid-modified nucleotide, is hydrolyzed by hMTH1, the human MutT homolog. PMID: 11852070 Role of tryptophan residues in the recognition of mutagenic oxidized nucleotides by human antimutator MTH1 protein PMID: 12051941 These results suggested that increased expression of hMTH in peripheral lymphocytes may be a risk factor for prostate cancer and support our priori hypothesis. PMID: 12619034 cleaves 8-oxo-dGTP to 8-oxo-GMP, an unusable form for DNA synthesis PMID: 12717453 Elevated levels of hMTH1 protein is asociated with non-small-cell lung carcinomas PMID: 12757855 MTH1 protects cells from H2O2-induced cell dysfunction and death by hydrolyzing oxidized purine nucleotides including 8-oxo-dGTP and 2-OH-dATP. PMID: 12857738 dGDP and dADP, at physiological concentrations not exceeding 5 microM and GDP at mean concentration of 30 microM, taken together, can decrease the cellular hMTH1 enzymatic activity vs. 8-oxo-dGTP PMID: 12957652 These results clarify the effects of the anti/syn conformation and the functional groups on the 2 and 6 positions of the purine ring on the recognition by the human MTH1 protein. PMID: 15095864 study presents the solution structure of Nudix family hydrolase MTH1 solved by multidimensional heteronuclear NMR spectroscopy PMID: 15133035 the Met allele at codon 83 of MTH1 gene might be involved in the development of type 1 diabetes mellitus in the Japanese female population. PMID: 15516784

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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