Cat: IPD-X41554

Recombinant Arabidopsis thaliana CAM4 Protein ,His & Myc

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Analytical Data

  • Gene name

    CAM4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (CaM-4)

  • Species

    Arabidopsis thaliana

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0DH96

  • Expression Region

    1-149aa

  • Molecular Weight

    24.3 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

CAM4, a peptide derived from the α-helical region of the C-terminus of cytochrome c, has garnered attention in the field of protein engineering and biotechnology due to its potential applications in therapeutic development and molecular biology. The protein's structural characteristics make it an ideal candidate for studying protein-protein interactions, cellular signaling pathways, and as a model for understanding heme-binding dynamics. Previous studies have demonstrated that CAM4 exhibits notable stability and biological activity, suggesting it could play a role in enhancing drug delivery systems or serve as a scaffold for novel protein design. The growing understanding of its unique properties, combined with advancements in recombinant DNA technology, allows researchers to produce CAM4 in various expression systems, facilitating large-scale production for experimental purposes. Investigating the functional implications of CAM4 and its derivatives can lead to the development of innovative therapeutic agents, contributing to fields such as cancer therapy and regenerative medicine. Overall, the research surrounding CAM4 recombinant proteins is not only crucial for elucidating fundamental biological mechanisms but also for translating these findings into applicable solutions in clinical settings.

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