Cat: IPD-X40271

Recombinant Penaeus sp. chains Protein ,His & SUMO

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Analytical Data

  • Gene name

    chains

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ; Sarcoplasmic calcium-binding protein; alpha-B and -A chains; SCP alpha chain

  • Species

    Penaeus sp.

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P02636

  • Expression Region

    1-192aa

  • Molecular Weight

    42 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

Chains recombinant proteins are widely studied due to their significant applications in various fields such as medicine, biotechnology, and research. The ability to produce proteins through recombinant DNA technology allows for the generation of highly specific proteins, which can be tailored for unique functions or therapeutic uses. Researchers have focused on chains recombinant proteins because they can facilitate the study of protein interactions, mechanisms, and functionalities at a molecular level. The advancements in techniques such as genetic engineering, protein expression systems, and purification methods have enhanced the efficiency and purity of these proteins. Furthermore, chains recombinant proteins are pivotal in the development of vaccines, enzymes, and antibodies, contributing to advancements in disease diagnostics and treatment. As our understanding of protein structure and function continues to evolve, the study of chains recombinant proteins holds the promise of innovations in therapeutic strategies, particularly in fields like cancer treatment and personalized medicine, where targeted therapies are crucial. Overall, the research into chains recombinant proteins is a dynamic area that bridges fundamental science and practical applications, driving progress in various biotechnological advancements.

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