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Recombinant Human Nicotinate phosphoribosyltransferase (NAPRT), Truncated

This Human NAPRT1 recombinant protein was produced in E.coli, where the gene sequence encoding Human NAPRT1 (229-538aa) was expressed with the N-terminal GST tag. The purity of this NAPRT1 protein was greater than 90% by SDS-PAGE.NAPRT is an enzyme that plays a crucial role in the nicotinic acid (niacin) metabolism pathway. Its primary function is to catalyze the reaction between nicotinic acid and phosphoribosyl pyrophosphate (PRPP), converting nicotinic acid into a precursor for nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP). NAD and NADP are essential coenzymes in cells, participating in various biological processes, including energy metabolism, DNA repair, antioxidant reactions, and more. Therefore, NAPRT plays a significant role in maintaining normal cellular metabolism and function. NAPRT is also important in anticancer drug research. Some anticancer drugs, such as quinolone-based medications, interfere with cell metabolism by affecting the activity of NAPRT, thereby exerting toxic effects on cancer cells.

ACP04471

This Human NAPRT1 recombinant protein was produced in E.coli, where the gene sequence encoding Human NAPRT1 (229-538aa) was expressed with the N-terminal GST tag. The purity of this NAPRT1 protein was greater than 90% by SDS-PAGE.NAPRT is an enzyme that plays a crucial role in the nicotinic acid (niacin) metabolism pathway. Its primary function is to catalyze the reaction between nicotinic acid and phosphoribosyl pyrophosphate (PRPP), converting nicotinic acid into a precursor for nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP). NAD and NADP are essential coenzymes in cells, participating in various biological processes, including energy metabolism, DNA repair, antioxidant reactions, and more. Therefore, NAPRT plays a significant role in maintaining normal cellular metabolism and function. NAPRT is also important in anticancer drug research. Some anticancer drugs, such as quinolone-based medications, interfere with cell metabolism by affecting the activity of NAPRT, thereby exerting toxic effects on cancer cells.

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Specifications


Cat.No ACP04471 Target NameNAPRT
FormLiquid or Lyophilized powderExpression SystemE.coli
Expression Range229-538aaMol Weight60.2kDa
Protein LengthPartialPurityGreater than 90% as determined by SDS-PAGE.
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ6XQN6
Background Information
  • Uniprot Id

    Q6XQN6

  • Target Species

    Human

  • Target Name

    NAPRT

  • Target Full Name

    Nicotinate phosphoribosyltransferase

  • Target Function

    Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.

  • Target Subcellular Location

    Cytoplasm, cytosol.

  • Target Protein Families

    NAPRTase family

  • Target Research Area

    Metabolism

  • Target Synonyms

    FHA HIT interacting protein; FHA-HIT-interacting protein; FHIP; NAPRT1; NAPRTase; Nicotinate phosphoribosyltransferase; Nicotinate phosphoribosyltransferase domain containing 1; Nicotinate phosphoribosyltransferase domain-containing protein 1; Nicotinic acid phosphoribosyltransferase; PNCB_HUMAN; PP3856

  • Target Background

    Nicotinic acid (NA; niacin) is converted by nicotinic acid phosphoribosyltransferase (NAPRT; EC 2.4.2.11) to NA mononucleotide (NaMN), which is then converted to NA adenine dinucleotide (NaAD), and finally to nicotinamide adenine dinucleotide (NAD), which serves as a coenzyme in cellular redox reactions and is an essential component of a variety of processes in cellular metabolism including response to stress (Hara et al., 2007).

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