Cat: IPD-X41157

Recombinant Clostridium acetobutylicum bcd Protein ,His & Myc

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Analytical Data

  • Gene name

    bcd

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Butyryl-CoA dehydrogenase SCAD

  • Species

    Clostridium acetobutylicum

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P52042

  • Expression Region

    1-379aa

  • Molecular Weight

    52.2 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

BCD (Bacterial Collagenase Domain) fusion proteins are an area of increasing research interest due to their potential applications in various fields, including medicine, biotechnology, and molecular biology. These proteins are characterized by their ability to facilitate the degradation of collagen and other extracellular matrix components, making them valuable in tissue engineering and regenerative medicine. The significance of studying BCD fusion proteins lies in their dual functionality; they can serve as tools for probing cellular processes and as therapeutic agents that promote wound healing and tissue repair. Additionally, BCD proteins can be utilized in the development of targeted drug delivery systems, enabling more precise treatment options for diseases such as cancer. The growing understanding of BCD structure-function relationships, along with advancements in genetic engineering techniques, allows for the optimization of these proteins for enhanced specificity and efficacy. Consequently, ongoing research aims to elucidate the mechanisms underlying BCD activity, explore their interactions with biological systems, and assess their safety and therapeutic potential in clinical applications. The multidisciplinary nature of this research encompasses biochemistry, molecular biology, and pharmacology, highlighting the importance of collaboration among scientists to advance the field and unlock the full potential of BCD fusion proteins in diverse applications.

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