Cat: IPD-X28625

Recombinant Human HSCB Protein,Strep & His

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Analytical Data

  • Gene name

    HSCB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DNAJC20; HSC20

  • Species

    Human

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8IWL3

  • Expression Region

    M1-L235

  • Protein Length

    Full Length

  • 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

HSCB, or Heat Shock Cognate Protein B, is a crucial molecular chaperone that plays a significant role in protein folding and cellular stress responses. Its primary function involves assisting in the proper folding of nascent proteins and the refolding of misfolded proteins, thereby preventing aggregation and promoting cellular homeostasis. The study of HSCB is particularly important in the context of various diseases, including neurodegenerative disorders and cancers, where protein misfolding and aggregation are common pathological features. Researchers have focused on the recombinant production of HSCB to gain insights into its structure-function relationship, investigate its interaction with other cellular components, and assess its potential as a therapeutic target. Recombinant proteins allow for detailed biophysical characterization and functional studies, which are essential for understanding the molecular mechanisms underlying HSCB's role in stress responses. Additionally, the development of HSCB-based therapeutics could pave the way for novel treatment strategies aimed at mitigating the detrimental effects of protein misfolding in affected cells. As a result, ongoing research into the recombinant expression and functional analysis of HSCB is vital to broaden our understanding of protein homeostasis and to explore new avenues for intervention in human diseases associated with proteostasis failure.

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