Cat: IPD-X39038

Recombinant Human CHERP Protein,His

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Analytical Data

  • Gene name

    CHERP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DAN16; SCAF6; SR-related CTD-associated factor 6

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8IWX8

  • Expression Region

    Met1~Ser186

  • Molecular Weight

    27kDa

  • 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

CHERP (calcium homeostasis endoplasmic reticulum protein) is an integral membrane protein primarily located in the endoplasmic reticulum (ER), playing a critical role in cellular calcium signaling and homeostasis. Research on CHERP has gained prominence due to its involvement in various physiological processes and disease states. Initial studies highlighted its function in regulating intracellular calcium levels, which are essential for various cellular activities, including muscle contraction, neurotransmitter release, and gene expression. Dysregulation of calcium signaling is linked to numerous pathological conditions, such as neurodegenerative diseases, cardiac dysfunction, and cancer. Notably, CHERP has been implicated in the modulation of apoptosis and stress responses, making it a potential target for therapeutic intervention. Investigating the overexpression and functional properties of recombinant CHERP has the potential to elucidate its mechanistic role in calcium signaling pathways and cellular stress responses. Furthermore, understanding the structural and functional dynamics of CHERP could pave the way for developing novel therapeutics aimed at restoring calcium homeostasis in diseases characterized by calcium dysregulation. Overall, the study of recombinant CHERP not only contributes to our fundamental understanding of calcium biology but also holds promise for advancing targeted therapies for related disorders.

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