Cat: IPD-X39972

Recombinant Human RBMX Protein ,GST

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Analytical Data

  • Gene name

    RBMX

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Glycoprotein p43 (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) (HNRPG) (RBMXP1)

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P38159

  • Expression Region

    333-391aa

  • Molecular Weight

    33.4 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.

Quality inspection process

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Protein Description

RBMX (RNA Binding Motif Protein 1) is a protein known for its role in RNA processing and regulation, making it an intriguing subject for both basic and applied research. It is involved in various cellular functions, including splicing, RNA stability, and transport, which are critical for maintaining cellular homeostasis. Dysregulation of RBMX has been implicated in several diseases, particularly cancer, where aberrant splicing patterns can lead to oncogenic alterations. Recent studies have highlighted its potential as a therapeutic target, prompting investigations into the structural and functional dynamics of RBMX. Researchers have begun exploring recombinant forms of RBMX to better understand its interactions with RNA and other cellular components. This approach not only aids in deciphering the molecular mechanisms underlying its function but also facilitates the development of novel strategies to modulate its activity in disease contexts. The recombination of RBMX provides insights into post-translational modifications and the impact of specific domains on its RNA-binding capabilities. As such, ongoing research in this area holds significant promise for advancing our understanding of RNA biology and developing innovative therapeutic interventions targeting RBMX-related pathways in various diseases.

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