Cat: PA2000-3379

Recombinant Human GEMIN7 Protein,His

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Analytical Data

  • Gene name

    GEMIN7

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GEMIN7;Gem-associated Protein 7

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9H840

  • Expression Region

    1-131aa

  • AA Sequence

    MQTPVNIPVPVLRLPRGPDGFSRGFAPDGRRAPLRPEVPEIQECPIAQESLESQEQRARAALRERYLRSLLAMVGHQVSFTLHEGVRVAAHFGATDLDVANFYVSQLQTPIGVQAEALLRCSDIISYTFKP

  • Molecular Weight

    41.5 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

The GEMIN7 protein, part of the GEMIN family, is a key player in the regulation of gene expression and RNA processing. Its involvement in the assembly and maturation of spliceosomal complexes makes it critical for pre-mRNA splicing. Recent research has revealed that GEMIN7 also interacts with various RNA-binding proteins, suggesting a broader role in RNA metabolism and cellular stress responses. Dysregulation of GEMIN7 has been linked to several diseases, including spinal muscular atrophy, where mutations in related proteins disrupt the normal functioning of the spliceosome. Understanding the structure and function of GEMIN7 is vital for uncovering its role in these pathways and could provide insights into novel therapeutic targets. Given its multifaceted role in RNA biology, the study of GEMIN7 and its interactions is essential for elucidating the complexities of gene regulation and disease pathology. Current research efforts are focusing on the structural characterization of GEMIN7 through techniques like X-ray crystallography and cryo-electron microscopy, as well as its interaction networks within the cell, to better understand how it contributes to RNA processing and what implications this has for human health and disease.

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