目录号 | 产品详情 | 靶点 | |
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T39334 | |||
Remdesivir nucleoside monophosphate, a metabolite of Remdesivir, is a potent antiviral compound with nucleoside analogue characteristics. It exhibits effective antiviral activity against both SARS-CoV and MERS-CoV. | |||
T19485 | Others | ||
Nucleoside-Analog-1 is a 4′-Azidocytidine analogue, used to against Hepatitis C virus replication. | |||
T24385 | |||
L-Acosamine nucleoside has antiviral activity against HIV and HSV-1. | |||
T25759 | |||
L-Ristosamine nucleoside shows antiviral activity. | |||
T19486 | Others | ||
Nucleoside-Analog-2 is a 4'-Azidocytidine analogue, used to against Hepatitis C virus (HCV) replication. | |||
T6065 | Akt HIV Protease DNA/RNA Synthesis | ||
Triciribine (NSC-154020) 是一种 DNA 合成抑制剂,也抑制 Akt 和 HIV-1/2,IC50分别为 130 nM 和 0.02-0.46 μM。 | |||
TNU1281 | Others | ||
P-2'-deoxyribose (P-Nucleoside) 是一种脱氧核糖,广泛存在于生物体内。 | |||
T76096 | |||
Purine nucleoside phosphorylase 是嘌呤代谢中的关键酶,参与嘌呤挽救途径。Purine nucleoside phosphorylase 缺乏导致 T 细胞功能受损。在无机正磷酸盐作为第二底物的存在下,Purine nucleoside phosphorylase 催化核糖和脱氧核糖核苷的糖苷键断裂,生成嘌呤碱和核糖(脱氧核糖)-1-磷酸。 | |||
T75409 | |||
Nucleoside hydrolase (IAGNH)为一种糖苷酶,专门催化核苷中N-糖苷键的裂解,从而促进核碱基与Rib的循环利用。 | |||
T16674 | Endogenous Metabolite | ||
Pseudouridine 是非编码 RNA 中丰富的修饰核苷,通过稳定 RNA 结构增强核糖体 RNA 和的转移 RNA 功能。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-02279 | Nucleoside phosphorylase/PNP Protein, Human, Recombinant (His) | Human | E. coli | ||
Purine nucleoside phosphorylase (PNP) is a purine-metabolizing enzyme that catalyzes the reversible phosphorolysis of 6-oxypurine (deoxy)nucleosides to their respective bases and (deoxy)ribose-1-phosphate. It is a key enzyme in the purine salvage pathway of mammalian cells. Purine nucleoside phosphorylase is a transferase that catalyzes the addition of phosphate and removal of a purine base from guanosine and similar nucleosides.PNP defects result in metabolic abnormalities and fatal T cell immunodeficiency. Purine nucleoside phosphorylase (PNP) is a target for leukemia, gout, and autoimmune disorders.
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TMPJ-01308 | ITPase Protein, Human, Recombinant (His) | Human | E. coli | ||
Inosine Triphosphate Pyrophosphatase (ITPase) is a cytoplasmic enzyme that belongs to the HAM1 NTPase family. ITPase hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP) and deoxyinosine triphosphate (dITP) to the monophosphate nucleotide (IMP) and diphosphate. The ITPase enzyme acts as a homodimer and does not distinguish between the deoxy- and ribose forms. ITPase probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Defects in ITPase is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.
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TMPY-00116 | MTH1 Protein, Human, Recombinant (His) | Human | E. coli | ||
NUDT1 (Nudix Hydrolase 1) is a Protein Coding gene. The protein encoded by this gene is an enzyme that hydrolyzes oxidized purine nucleoside triphosphates to monophosphates, thereby preventing misincorporation. The NUDT1 protein is localized mainly in the cytoplasm, with some in the mitochondria, suggesting that it is involved in the sanitization of nucleotide pools both for nuclear and mitochondrial genomes. Cancers can survive the oxidative conditions by upregulating nucleoside diphosphate linked moiety X-type motif 1 (NUDT1). MiR-485-5p acts as a tumor suppressor by targeting NUDT1 in gastric cancer (GC). The miR-485-5p/NUDT1 axis is involved in the processes of cell growth and cell motility and plays a key role in the tumorigenesis of GC.
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TMPY-02278 | NUDT2 Protein, Human, Recombinant (His) | Human | E. coli | ||
NUDT2 Protein, Human, Recombinant (His) is expressed in E. coli with His tag. The predicted molecular weight is 18.3 kDa. Accession number: P50583
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TMPY-03849 | NUDT5 Protein, Human, Recombinant (His) | Human | E. coli | ||
NUDT5 (Nudix Hydrolase 5) is a Protein Coding gene. This gene belongs to the Nudix (nucleoside diphosphate linked moiety X) hydrolase superfamily. The encoded enzyme catalyzes the hydrolysis of modified nucleoside diphosphates. ADP-sugar Pyrophosphatase, also known as NUDT5, eliminates toxic nucleotide derivatives from the cell and regulates the levels of important signaling nucleotides and their metabolites. It is widely expressed in the liver, skin, and other tissues. NUDT5 functions as a MutT-related protein and catalyzes the hydrolysis of 8-oxoGDP to 8-oxoGMP, thereby preventing misincorporation of 8-oxoGua into RNA. NUDT5 may play significant roles in regulating the G1-S transition in mammalian cells. It can also hydrolyze other nucleotide sugars with low activity.
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TMPY-04467 | NME1 Protein, Human, Recombinant (His) | Human | E. coli | ||
NME1, also known as Nucleoside Diphosphate Kinase A (NDK-A), or NM23-H1, belongs to the NDK family. NM23-H1 is known to have a metastasis suppressive activity in many tumor cells. Recent studies have shown that the interacting proteins with NM23-H1 which mediate cell proliferation, may act as modulators of the metastasis suppressor activity. The interacting proteins with NM23-H1 can be classified into 3 groups. The first group of proteins can be classified as upstream kinases of NM23-H1 such as CKI and Aurora-A/STK15. The second group of proteins acts as downstream effectors for the regulation of specific gene transcriptions, GTP-binding protein functions, and signal transduction in the Erk signal cascade. The third group of proteins can be classified as bi-directionally influencing binding partners of NM23-H1. As a result, the interactions with NM23-H1 and binding partners have implications in the biochemical characterization involved in metastasis and tumorigenesis. NDKA is increased in human postmortem cerebrospinal fluid (CSF), a model of global brain insult, suggesting that measurement in CSF and, more importantly, in plasma may be useful as a biomarker of stroke. Additionally, NM23-H1 significantly reduces metastasis without effects on primary tumor size and was the first discovered metastasis suppressor gene.
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TMPH-01631 | DCP2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts.
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TMPH-03284 | CD39 Protein, Rat, Recombinant (E. coli, His) | Rat | E. coli | ||
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
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TMPH-03283 | CD39 Protein, Rat, Recombinant (His) | Rat | Baculovirus | ||
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
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TMPY-02929 | ENTPD2 Protein, Human, Recombinant (aa 29-460, His) | Human | Baculovirus-Insect Cells | ||
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.
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TMPY-05151 | CD39 Protein, Cynomolgus, Rhesus, Recombinant (His) | Cynomolgus,Rhesus | Baculovirus-Insect Cells | ||
CD39, also known as ENTPD1, belongs to the GDA1/CD39 NTPase family. It is expressed primarily on activated lymphoid cells and can also be detected in endothelial tissues. The vascular isoform and the placental isoform II are present in both placenta and umbilical vein, whereas placental isoform I is present in placenta only. CD39 can hydrolyze both nucleoside triphosphates and diphosphates. It is the dominant ecto nucleotidase of vascular and placental trophoblastic tissues and appears to modulate the functional expression of type 2 purinergic (P2) G protein coupled receptors (GPCRs). CD39 transgenic mice exhibit impaired platelet aggregation, prolonged bleeding times, and resistance to systemic thromboembolism. There is a correlation between ATP hydrolysis and triglycerides in patients with chronic heart disease, suggesting a relationship between ATP diphosphohydrolase and thrombogenesis. In the nervous system, CD39 could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission.
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TMPY-01126 | CD39 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
CD39, also known as ENTPD1, belongs to the GDA1/CD39 NTPase family. It is expressed primarily on activated lymphoid cells and can also be detected in endothelial tissues. The vascular isoform and the placental isoform II are present in both placenta and umbilical vein, whereas placental isoform I is present in placenta only. CD39 can hydrolyze both nucleoside triphosphates and diphosphates. It is the dominant ecto nucleotidase of vascular and placental trophoblastic tissues and appears to modulate the functional expression of type 2 purinergic (P2) G protein coupled receptors (GPCRs). CD39 transgenic mice exhibit impaired platelet aggregation, prolonged bleeding times, and resistance to systemic thromboembolism. There is a correlation between ATP hydrolysis and triglycerides in patients with chronic heart disease, suggesting a relationship between ATP diphosphohydrolase and thrombogenesis. In the nervous system, CD39 could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission.
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TMPY-02808 | CD39 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
CD39, also known as ENTPD1, belongs to the GDA1/CD39 NTPase family. It is expressed primarily on activated lymphoid cells and can also be detected in endothelial tissues. The vascular isoform and the placental isoform II are present in both placenta and umbilical vein, whereas placental isoform I is present in placenta only. CD39 can hydrolyze both nucleoside triphosphates and diphosphates. It is the dominant ecto nucleotidase of vascular and placental trophoblastic tissues and appears to modulate the functional expression of type 2 purinergic (P2) G protein coupled receptors (GPCRs). CD39 transgenic mice exhibit impaired platelet aggregation, prolonged bleeding times, and resistance to systemic thromboembolism. There is a correlation between ATP hydrolysis and triglycerides in patients with chronic heart disease, suggesting a relationship between ATP diphosphohydrolase and thrombogenesis. In the nervous system, CD39 could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission.
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TMPH-02964 | UMP-CMP kinase/CMPK1 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.
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TMPK-00852 | ENPP1 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression.
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TMPK-00854 | ENPP1 Protein, Human, Recombinant (C-His) | Human | HEK293 | ||
Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression.
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TMPK-00781 | ENPP1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression.
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TMPK-00853 | ENPP1 Protein, Human, Recombinant (N-His) | Human | HEK293 | ||
Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression.
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TMPH-00099 | NDK1 Protein, Arabidopsis thaliana, Recombinant (His & Myc) | Arabidopsis thaliana | Yeast | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Plays a role in response to reactive oxygen species (ROS) stress.
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TMPH-03452 | NDPK Protein, S. cerevisiae, Recombinant (His) | Saccharomyces cerevisiae | Yeast | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage.
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TMPH-03451 | NDPK Protein, S. cerevisiae, Recombinant (E. coli, His) | Saccharomyces cerevisiae | E. coli | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage.
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TMPH-01211 | DGUOK Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Phosphorylates deoxyguanosine and deoxyadenosine in the mitochondrial matrix, with the highest efficiency for deoxyguanosine. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK and TK2. Phosphorylates certain nucleoside analogs. Widely used as target of antiviral and chemotherapeutic agents.
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TMPY-02758 | ENTPD5 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Ectonucleoside triphosphate diphosphohydrolase 5 (ENTPD5), also known as CD39 antigen-like 4, ER-UDPase, Guanosine-diphosphatase ENTPD5, Nucleoside diphosphatase Uridine-diphosphatase ENTPD5. This hydrolase is expressed in response to phosphoinositide 3-kinase (PI3K) signaling. Activation of PI3K results in FOXO phosphorylation by AKT1 and loss of ENTPD5 transcriptional repression. It is Up-regulated in PTEN-deficient cells. Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation.ENTPD5 promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, ENTPD5 constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. ENTPD5 also hydrolyzes GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. This enzyme Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.
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TMPY-03617 | GMPR Protein, Human, Recombinant (His) | Human | E. coli | ||
GMPR, also known as GMPR1, belongs to the IMPDH/GMPR family.This familyofenzymesincludesIMP dehydrogenaseandGMP reductase. These enzymes are involved inpurine metabolism and adopt aTIM barrelstructure. GMPR is an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP. GMPR functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
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TMPY-04276 | ENTPD5 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Ectonucleoside triphosphate diphosphohydrolase 5 (ENTPD5), also known as CD39 antigen-like 4, ER-UDPase, Guanosine-diphosphatase ENTPD5, Nucleoside diphosphatase Uridine-diphosphatase ENTPD5. This hydrolase is expressed in response to phosphoinositide 3-kinase (PI3K) signaling. Activation of PI3K results in FOXO phosphorylation by AKT1 and loss of ENTPD5 transcriptional repression. It is Up-regulated in PTEN-deficient cells. Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation.ENTPD5 promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, ENTPD5 constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. ENTPD5 also hydrolyzes GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. This enzyme Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.
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TMPH-00713 | Polyphosphate kinase Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG) synthesis and autophosphorylation.
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TMPY-04480 | UMP-CMP kinase/CMPK1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
CMPK1 plays a key role in the maintenance of pyrimidine nucleotide pool profile and for the metabolism of pyrimidine analogs in cells. It catalyzes the phosphoryl transfer from ATP to UMP, CMP, and deoxy-CMP (dCMP), resulting in the formation of ADP and the corresponding nucleoside diphosphate. CMPK1 also has a significant role in the activation of pyrimidine analogs, which are clinically useful anti-cancer and anti-viral drugs. In the meanwhile, CMPK1 functions in cellular nucleic acid biosynthesis.
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TMPJ-01406 | MOB4 Protein, Human, Recombinant (His) | Human | E. coli | ||
MOB-Like Protein Phocein is a member of the MOB1/Phocein Family. MOB-Like Protein Phocein is associated with membranes and the Golgi stacks. It is present in the cytosol, where it behaves as a protein complex. It has been shown that MOB-Like Protein Phocein interacts with DNM1, EPS15 and Nucleoside Diphosphate Kinase. MOB-Like Protein Phocein is the major partner of Striatin Family members and may play a important role in membrane trafficking, specifically in membrane budding reactions.
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TMPJ-00922 | DCK Protein, Human, Recombinant (His & T7) | Human | E. coli | ||
Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localized to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.
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TMPY-03330 | BPHL Protein, Human, Recombinant (His) | Human | E. coli | ||
BPHL is a member of the serine protease family. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. It catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. BPHL also activates valacyclovir to acyclovir. It may play a role in detoxification processes.
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TMPJ-00496 | PGM2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Phosphoglucomutase-2 (PGM2) is a member of PGM family, which catalyzes the inter-conversion of sugar phosphates and participates in anabolic and catabolic reactions. When cells are grown in glucose, PGM catalyzes the conversion of glucose-6-phosphate to glucose-1-phosphate an important precursor required for the synthesis of UDP glucose and trehalose. PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses, and it may also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. But this protein has low glucose 1,6-bisphosphate synthase activity.
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TMPH-00609 | dITP/XTP pyrophosphatase Protein, E. coli, Recombinant (His & Myc & SUMO) | E. coli | E. coli | ||
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Can also efficiently hydrolyze 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP). Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. To a much lesser extent, is also able to hydrolyze GTP, dGTP and dUTP, but shows very low activity toward the canonical nucleotides dATP, dCTP and dTTP and toward 8-oxo-dGTP, purine deoxyribose triphosphate, 2-aminopurine deoxyribose triphosphate and 2,6-diaminopurine deoxyribose triphosphate.
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TMPY-03508 | XTP3TPA Protein, Human, Recombinant (His) | Human | E. coli | ||
DCTPP1 hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. It has a strong preference for modified dCTP. DCTPP1’s activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. DCTPP1 also hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). DCTPP1 does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. It may protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. DCTPP1 may also protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.
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TMPJ-00682 | CD39L1 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
CD39L1 protein (ENTPD2 or NTPDase2) is a member of the ecto-nucleoside triphosphate diphosphohydrolase family which the main role is termination of purinergic signaling. CD39L1 gene encodes a precursor protein with 495 amino acid residues which generates a 437 amino acid residues mature protein after processing. It is an ecto-nucleotidase that found on the surface of vascular adventitial cells and accessory vascular cells. CD39L1 is a Ca2+- and Mg2+-dependent enzyme that activates platelets by preferentially converting ATP to ADP. CD39L1 plays a role in regulating thrombosis and inflammation which is considered to be a therapeutic target for thromboregulation and the treatment of vascular inflammation. Alternative splicing of CD39L1 gene results in multiple transcript variants.
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TMPY-02975 | CANT1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CANT1(calcium activated nucleotidase 1) belongs to the apyrase family. Apyrase is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP: ADP and another with no selectivity. It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate. CANT1 functions as a calcium-dependent nucleotidase with a preference for UDP. Defects in CANT1 are the cause of desbuquois dysplasia.
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TMPY-02893 | NT5C3A/NT5C3 Protein, Human, Recombinant | Human | E. coli | ||
NT5C3A (5'-Nucleotidase, Cytosolic IIIA) is a Protein Coding gene. This gene encodes a member of the 5'-nucleotidase family of enzymes that catalyze the dephosphorylation of nucleoside 5'-monophosphates. The encoded protein is the type 1 isozyme of pyrimidine 5' nucleotidase and catalyzes the dephosphorylation of pyrimidine 5' monophosphates. NT5C3A expression required both an intronic IFN-stimulated response element and the IFN-stimulated transcription factor IRF1. Overexpression of NT5C3A, but not of its catalytic mutants, suppressed IL-8 production by HEK293 cells. NT5C3A-stimulated sirtuin activity resulted in deacetylation of histone H3 and the NF-kappaB subunit RelA (also known as p65), both of which were associated with the proximal region of the Il8 promoter, thus repressing the transcription of Il8 Together.
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TMPH-01801 | NME2 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity.
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TMPY-02710 | CANT1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CANT1(calcium activated nucleotidase 1) belongs to the apyrase family. Apyrase is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP: ADP and another with no selectivity. It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate. CANT1 functions as a calcium-dependent nucleotidase with a preference for UDP. Defects in CANT1 are the cause of desbuquois dysplasia.
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TMPH-03205 | HINT1 Protein, Rabbit, Recombinant (His & Myc) | Rabbit | HEK293 | ||
Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Hydrolyzes adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase. Hydrolyzes Met-AMP, His-AMP, Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Also exhibits SUMO-specific isopeptidase activity, deconjugating SUMO1 from RANGAP1 and RGS17.
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TMPH-00568 | 8-oxo-dGTP diphosphatase Protein, E. coli, Recombinant (His & SUMO) | E. coli | E. coli | ||
Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT may also ensure transcriptional fidelity, removing 8-oxo-GTP from the ribonucleotide triphosphate pool. However, due to the lower efficiency of RNA polymerase 8-oxo-GTP incorporation, MutT is probably not a major contributor to transcriptional fidelity. It also hydrolyzes 8-oxo-dGDP and 8-oxo-GDP to their monophosphate form. In vitro, can also use dGTP, dGDP and other various nucleoside di- and triphosphates, with much lower efficiency. Works cooperatively with MutM and MutY to prevent accumulation in the DNA of oxidized guanine residues.
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TMPH-01802 | NME4 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling.
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