Cat: IPD-X39006

Recombinant Mouse BAG4 Protein,His

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Analytical Data

  • Gene name

    BAG4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SODD; Silencer Of Death Domains; BAG family molecular chaperone regulator 4

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8CI61

  • Expression Region

    Ser210~Ala447

  • Molecular Weight

    35&33kDa

  • 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

BAG4, a member of the BAG (BCL2-associated athanogene) family, plays a crucial role in regulating cellular stress responses, apoptosis, and protein homeostasis. Research on BAG4 has gained momentum due to its potential implications in various diseases, including cancer and neurodegenerative disorders. Unlike its relatives, BAG4 has unique properties that allow it to interact with multiple signaling pathways and molecular chaperones, particularly Hsp70 and Hsp90, which are vital in managing protein folding and degradation. Investigating BAG4's structure and function can reveal insights into its mechanisms in cellular contexts and its involvement in disease progression. The reconstitution of BAG4 as a recombinant protein is essential for elucidating its biochemical properties, facilitating the study of its interactions, and assessing its functional roles. Furthermore, as BAG4 has been implicated in promoting cell survival under stress conditions, understanding its molecular dynamics could pave the way for novel therapeutic strategies targeting BAG4 in various pathological states. Thus, the study of recombinant BAG4 protein is critical for advancing our knowledge of its biological functions and therapeutic potential.

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