Cat: IPD-X38520

Recombinant Human CAPS Protein,His

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Analytical Data

  • Gene name

    CAPS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CAPS1; Thyroid Protein p24; Calcyphosin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q13938

  • Expression Region

    Met1~Leu189

  • Molecular Weight

    25kDa

  • 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

CAPS (Ca2+-dependent Activator Protein for Secretion) is a crucial protein involved in the regulated exocytosis of neurotransmitters and hormones, playing a significant role in neuronal communication and endocrine functions. Its influence on the fusion of secretory vesicles with the plasma membrane has garnered considerable interest in the fields of cell biology and neuroscience. Research indicates that CAPS acts as a mediator by linking calcium signaling to the exocytotic machinery, thereby facilitating the rapid release of synaptic vesicles in response to calcium influx. This process is essential for neurotransmitter release at synapses, influencing synaptic plasticity and overall neural transmission. The dysregulation of CAPS function has been implicated in various neurological disorders and endocrine pathologies, making it a potential therapeutic target. Consequently, understanding the molecular mechanisms of CAPS, including its interactions with other proteins and its regulatory pathways, is vital. Recent studies employing advanced techniques, such as cryo-electron microscopy and high-resolution imaging, have begun to elucidate the structural dynamics of CAPS in action, providing insights into its conformational changes during vesicle fusion. Ongoing research aims to unravel the specific roles of CAPS in different cell types and under various physiological and pathological conditions, thereby contributing to a deeper understanding of exocytosis and its implications for health and disease.

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