Cat: IPD-X40628

Recombinant Human AMDHD1 Protein ,His & SUMO

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Analytical Data

  • Gene name

    AMDHD1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Amidohydrolase domain-containing protein 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96NU7

  • Expression Region

    1-426aa

  • Molecular Weight

    62.7 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.

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Protein Description

AMDHD1 (Acyl-Modified Domain-Containing Protein 1) is a member of the acyl-activating enzyme family, which plays a crucial role in lipid metabolism and signaling pathways. Research on AMDHD1 has gained attention due to its potential implications in various biological processes and diseases, including metabolic disorders and cancer. The enzyme is involved in the acylation of specific substrates, influencing cellular functions and the regulation of signaling pathways. Recent studies have focused on elucidating its structural characteristics and enzymatic mechanisms, revealing insights into how AMDHD1 modulates lipid homeostasis and contributes to cellular signaling networks. Moreover, its dysregulation has been implicated in pathological conditions, making it a target of interest for therapeutic interventions. Understanding the functional role of AMDHD1 could pave the way for novel strategies in targeting metabolic diseases and developing potential biomarkers for cancer progression, highlighting its significance in both basic and applied biomedical research.

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