Cat: IPD-X39862

Recombinant Human INMT Protein ,His & SUMO

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Analytical Data

  • Gene name

    INMT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Aromatic alkylamine N-methyltransferase ;Amine N-methyltransferase ;Arylamine N-methyltransferaseThioether S-methyltransferase ;TEMT

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O95050

  • Expression Region

    1-263aa

  • Molecular Weight

    44.9 kDa

  • 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

INMT (Indolethylamine N-methyltransferase) is an essential enzyme involved in the biosynthesis of biologically active compounds such as neurotransmitters and indole derivatives. This enzyme catalyzes the N-methylation of indoleamine substrates, playing a crucial role in the metabolism of serotonin and other tryptophan derivatives. Dysregulation of INMT has been implicated in various neurological and psychiatric disorders, making it a significant target for research in medicinal chemistry and neurobiology. Recent studies have explored the potential of recombinant INMT proteins for therapeutic applications, as well as their role in elucidating metabolic pathways associated with indole compounds. The advancement of recombinant DNA technology has facilitated the production and characterization of INMT, enabling systematic investigations into its enzymatic properties and regulatory mechanisms. Understanding the structure-function relationship of INMT through recombinant protein studies could illuminate its role in human health and disease, paving the way for novel pharmacological strategies aimed at modulating its activity for therapeutic benefit. The ongoing research endeavors emphasize the importance of INMT as a vital component of the biochemical landscape and its potential exploitation in drug discovery and development.

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