Cat: IPD-X28565

Recombinant Human DNAJC9 Protein,Strep & His

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Analytical Data

  • Gene name

    DNAJC9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DnaJ homolog subfamily C member 9; DnaJ protein SB73; DNAJC9; Homo sapiens; Human; Chaperone

  • Species

    Human

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8WXX5

  • Expression Region

    G2-K260

  • Protein Length

    Partial

  • 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

DNAJC9, a member of the DNAJ/HSP40 family of proteins, has garnered significant attention in recent years due to its critical role in protein homeostasis and cellular stress responses. As a co-chaperone, DNAJC9 interacts with Hsp70, facilitating the proper folding and assembly of nascent polypeptides, as well as the refolding of misfolded proteins. Research has revealed that DNAJC9 plays a vital role in various cellular processes, including the regulation of immune responses, apoptosis, and the maintenance of proteostasis. Abnormal expression or mutations in DNAJC9 have been implicated in several diseases, including neurodegenerative disorders and cancer, highlighting its potential as a therapeutic target. Studies using recombinant DNAJC9 have aimed to elucidate its molecular mechanisms and interactions, offering insights into how it contributes to cellular health and disease. Furthermore, understanding the functional dynamics of DNAJC9 may lead to the development of novel strategies to modulate its activity, paving the way for innovative therapeutic approaches in treating diseases associated with proteostasis dysfunction. As such, the research surrounding DNAJC9 and its recombinant protein form is increasingly relevant for advancing our understanding of cellular biology and potential clinical applications.

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