Cat: IPD-X32417

Recombinant Human MINDY1 Protein (Baculovirus),GST

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Analytical Data

  • Gene name

    MINDY1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FAM63A; KIAA1390

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N-GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8N5J2-1

  • Expression Region

    M1-L469

  • Protein Length

    Full Length of Isoform-1

  • Molecular Weight

    95 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.

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Protein Description

MINDY1 is a member of the mitochondrial dynamin-like GTPases, which are critical for mitochondrial fission and fusion processes. Recent research has highlighted the importance of MINDY1 in regulating mitochondrial dynamics, and its role in maintaining cellular homeostasis. Mitochondria are vital for energy production and are implicated in numerous diseases, including neurodegenerative disorders, cancer, and metabolic syndromes. Dysregulation of mitochondrial dynamics, such as excessive fission or impaired fusion, can lead to cellular dysfunction and contribute to these diseases. The study of MINDY1 and its recombinant proteins has gained attention as a potential therapeutic target, as understanding its function may provide insights into the underlying mechanisms of mitochondrial-related pathologies. Researchers have developed various recombinant forms of MINDY1 to elucidate its biochemical properties, interaction with other mitochondrial proteins, and its regulatory roles in mitochondrial morphology and function. This work seeks to establish MINDY1 as a significant player in mitochondrial biology, potentially offering new avenues for therapeutic intervention in diseases associated with mitochondrial dysfunction. Through advanced techniques such as CRISPR/Cas9 gene editing, mass spectrometry, and high-resolution microscopy, the functional characterization of MINDY1 continues to grow, paving the way for targeted strategies aimed at modulating mitochondrial dynamics in various clinical contexts. Understanding MINDY1's molecular mechanisms could ultimately inform the development of novel treatments aimed at restoring proper mitochondrial function and mitigating the effects of mitochondrial diseases.

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