Cat: IPD-X27119

Recombinant Human Nicotinamide N-Methyltransferase/NNMT Protein,His

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Analytical Data

  • Gene name

    Nicotinamide N-Methyltransferase/NNMT

  • 简介

    The nicotinamide N-methyltransferase (NNMT) protein catalyzes the methylation of nicotinamide using S-adenosyl-L-methionine to form N1-methylnicotinamide. NNMT affects pluripotent embryonic stem cell development and acts as a metabolic regulator, affecting adipose tissue energy expenditure, gluconeogenesis, and cholesterol biosynthesis. Nicotinamide N-Methyltransferase/NNMT Protein, Human (His) is the recombinant human-derived Nicotinamide N-Methyltransferase/NNMT protein, expressed by E. coli , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    1. Measured in a cell proliferation assay using A549 cells. The ED50 for this effect is 0.0488 μg/mL, corresponding to a specific activity is 2.049×104 units/mg. 2. Measured by its ability to methylate nicotinamide. The specific activity is 114.696 pmol/min/μg. Measured in a cell proliferation assay using A549 cells. The ED50 for this effect is 0.0488 μg/mL, corresponding to a specific activity is 2.049×104 units/mg.

  • Alternative Names

    Nicotinamide N-methyltransferase; NNMT

  • Species

    Human

  • Source

    E. coli

  • Tag

    C-6*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P40261

  • Expression Region

    M1-L264

  • AA Sequence

    MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLSRPL

  • Protein Length

    Full Length

  • Molecular Weight

    25-30

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

Nicotinamide N-methyltransferase (NNMT) is an important enzyme involved in the metabolism of nicotinamide, which plays a crucial role in various biological processes, including energy metabolism and cellular signaling. Elevated levels of NNMT have been associated with several metabolic disorders, including obesity and type 2 diabetes, making it a potential therapeutic target. Additionally, NNMT has been implicated in cancer progression and drug metabolism due to its role in modulating the availability of nicotinamide coenzymes and methyl groups. The recombinant protein form of NNMT is especially significant for research, as it allows for detailed studies of its enzymatic properties, substrate specificity, and inhibitor design. Understanding NNMT's structure-function relationship can provide insight into its biological roles and facilitate the development of novel pharmacological strategies for metabolic diseases and cancer. Therefore, producing and characterizing recombinant NNMT is a critical step in elucidating its function and therapeutic potential. Researchers employ various techniques, including molecular cloning and expression systems, to obtain functional NNMT, which can then be used in biochemical assays to explore its activity and regulation in different physiological contexts. Overall, the study of recombinant NNMT is essential for advancing our understanding of its role in human health and disease.

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