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NUDT9 hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.

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ADSSL1 is a muscle isozyme of adenylosuccinate synthase (EC 6.3.4.4), which catalyzes the initial reaction in the conversion of inosine monophosphate (IMP) to adenosine monophosphate (AMP).

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FUNCTION: Produces green light with a wavelength of 562 nM.
CATALYTIC ACTIVITY: Photinus luciferin + O₂ + ATP = oxidized Photinus luciferin + CO₂ + AMP + diphosphate + light.
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
COFACTOR: Magnesium.
SUBCELLULAR LOCATION: Peroxisomal.

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FUNCTION: Membrane-bound, calcium-inhibitable adenylyl cyclase (By similarity).
CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
SIMILARITY: Contains 2 guanylate cyclase domains.
COFACTOR: Binds 2 magnesium ions per subunit (By similarity).

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalysing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It can use both glutamine or ammonia as a nitrogen source. Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H₂O = AMP + diphosphate + NAD+ + L-glutamate.

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CANT1 belongs to the apyrase family.It is a calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. The enzyme has very low activity towards ADP and even lower activity towards ATP. And it does not hydrolyze AMP and GMP.

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AMPD3 is a member of the AMP deaminase gene family. It is a highly regulated enzyme that catalyses the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in the gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. [RefSeq].

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalyzing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It was shown to be induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation and is involved in biological processes like stress response and sporulation resulting in formation of a cellular spore. Catalytic activity: ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+

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NadN (NAD nucleotidase) is a periplasmic enzyme from Haemophilus influenzae, a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. NadN plays a central role by degrading NAD into adenosine and NR (nicotinamide riboside), NMN to nicotinamide riboside and AMP to adenosine. It shows a broad substrate specificity, recognising either mono- or di-nucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. It can be used as an economically alternative to produce NR (nicotinamide riboside). Catalytic activity: NAD=AMP + NMN=Ade+NR+PPi | AMP=Ade+Pi | NMN=NR+Pi.

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

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CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD).

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L-glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. The metabotropic glutamate receptors are a family of G protein-coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. GRM6 is part of Group III which is linked to the inhibition of the cyclic AMP cascade.

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The process of transferring lipoic acid to proteins is a two-step process. The first step is the activation of lipoic acid by lipoate-activating enzyme to form lipoyl-AMP. For the second step, LIPT1 transfers the lipoyl moiety to apoproteins.The process of transferring lipoic acid to proteins is a two-step process. The first step is the activation of lipoic acid by lipoate-activating enzyme to form lipoyl-AMP. For the second step, the protein encoded by this gene transfers the lipoyl moiety to apoproteins. Alternative splicing in the 5' UTR of this gene results in five transcript variants that encode the same protein.

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Inositol monophosphatase 2, also known as Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2 and IMPA2, is an enzyme which belongs to the inositol monophosphatase family. IMPA2 catalyses the dephosphoylration of inositol monophosphate with cofactor Magnesium and Inhibited by high Li+ and restricted Mg2+ concentrations. IMPA2 plays an important role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain, it is considered to have a role in schizophrenia and bipolar disorder.

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CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD).

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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ACSBG2 belongs to the ATP-dependent AMP-binding enzyme family, bubblegum subfamily.ACSBG2 mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. It is able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. ACSBG2 has increased ability to activate oleic and linoleic acid. It may play a role in spermatogenesis.

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SIK3 Antibody: Salt-inducible kinase family (SIKs) proteins are thought to have a role in steroidogenesis, adipogenesis or regulation of tumor malignancy. Three members (SIK1, SIK2 and SIK3) in the SIK family have been identified thus far. Their kinase domain sequences are closely homologous to those of AMP-activated protein kinase (AMPK). SIK3 can be phosphorylated by a tumor-suppressor kinase LKB1. It is highly and preferentially expressed in ovarian tumors but not in adenomyosis and leiomyoma and may be a potential diagnostic marker for ovarian cancers.

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The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD (Zhang et al., 2003 [PubMed 12574164]).

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This gene is a member of the type IV, cyclic AMP (cAMP)-specific, cyclic nucleotide phosphodiesterase (PDE) family. Cyclic nucleotides are important second messengers that regulate and mediate a number of cellular responses to extracellular signals, such as hormones, light, and neurotransmitters. The cyclic nucleotide phosphodiesterases (PDEs) regulate the cellular concentrations of cyclic nucleotides and thereby play a role in signal transduction. This gene encodes a protein that specifically hydrolyzes cAMP. Altered activity of this protein has been associated with schizophrenia and bipolar affective disorder. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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2'-PDE is an enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. 2'-PDE also cleaves 3',5'-phosphodiester bond of oligoadenylates. 2'-PDE play a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system.

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The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

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Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localisation, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerisation and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyses the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

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PRKAA1 belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.

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Adenine phosphoribosyltransferase (APRT) belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.Adenine phosphoribosyltransferase belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.

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HINT1 Antibody: Histidine triad nucleotide-binding protein 1 (HINT1) is a member of the histidine triad (HIT) protein family, a group of small nucleotide-binding and -hydrolyzing proteins. HINT1 interacts with several diverse proteins and has been suggested to have tumor suppressive activities. HINT1 catalyzes the hydrolysis of adenosine 5'-monophoramidate substrates such as AMP-morpholidate, but its enzymatic function does not appear to play a role in its tumor suppression. Recent experiments demonstrate that HINT1 forms a complex with POSH and JNK in vivo, inhibiting AP-1 activity and the phosphorylation of c-Jun, and this action could contribute to the tumor suppressor activity of HINT1. Other studies raise the possibility of HINT1 as a candidate gene for schizophrenia.

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PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.

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PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.