Cat: IPD-X40878

Recombinant Human ZNF592 Protein ,GST

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Analytical Data

  • Gene name

    ZNF592

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ZNF592; KIAA0211; Zinc finger protein 592

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q92610

  • Expression Region

    1-242aa

  • Molecular Weight

    53.2 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

ZNF592, a member of the zinc finger protein family, has gained attention in recent years due to its potential roles in gene regulation and cellular processes. Research indicates that ZNF592 may be implicated in various biological pathways, including development, differentiation, and response to stress. Its structure, characterized by multiple zinc finger motifs, suggests a function in DNA binding and transcriptional regulation. Studies have shown that alterations in ZNF592 expression are associated with several diseases, including cancer, highlighting its significance as a potential biomarker and therapeutic target. The generation of recombinant ZNF592 protein allows for detailed functional studies, enabling researchers to elucidate its precise biological roles and interactions at the molecular level. Understanding ZNF592's mechanisms could provide insights into its contributions to cellular physiology and pathology, paving the way for novel strategies in disease intervention and treatment.

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