Cat: IPD-X41826

Recombinant Escherichia coli csgB Protein,Avi & His

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Analytical Data

  • Gene name

    csgB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- MBP & C- His-Avi

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0ABK7

  • Expression Region

    22-151aa

  • Molecular Weight

    61.5 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

CSGB (Cobalt Sulfide Gene B) recombinant protein research has garnered significant attention due to its potential applications in biotechnology and medicine. CSGB plays a critical role in various biological processes, particularly in microbial metabolism and bioremediation, where it contributes to the detoxification of heavy metals and other environmental pollutants. The ability to express and purify CSGB in a recombinant form allows researchers to study its structure-function relationships and enzymatic activities in detail. Advances in molecular cloning and protein expression systems have facilitated the production of large quantities of this protein, enabling in-depth biochemical analyses and functional assays. Furthermore, understanding the mechanisms through which CSGB operates can lead to innovative strategies for environmental cleanup and the development of sustainable biotechnological processes. The potential for CSGB to be utilized in biomaterials and drug delivery systems highlights its versatility and significance in modern science. Therefore, ongoing research aims to elucidate the molecular characteristics of CSGB, paving the way for its application in both industrial and therapeutic contexts.

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