Cat: PA2000-2587

Recombinant E.coli MALD1 Protein,His

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Analytical Data

  • Gene name

    MALD1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MALD1;MRVLDC1;MARVEL domain-containing Protein 1

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P43211

  • Expression Region

    2-159aa

  • AA Sequence

    GVYTFENEFTSEIPPSRLFKAFVLDADNLIPKIAPQAIKQAEILEGNGGPGTIKKITFGEGSQYGYVKHRIDSIDEASYSYSYTLIEGDALTDTIEKISYETKLVACGSGSTIKSISHYHTKGNIEIKEEHVKVGKEKAHGLFKLIESYLKDHPDAYN

  • Molecular Weight

    33.5 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.

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Protein Description

MALD1, or "MAL domain-containing protein 1," has emerged as a significant focus in biological research due to its potential roles in various cellular processes, including cell signaling, immune response, and disease pathogenesis. The MALD1 protein, characterized by the presence of a MAL domain, is involved in the modulation of protein interactions and cellular pathways. Recent studies suggest that MALD1 may play a crucial role in cancer biology, particularly in tumor metastasis and immune evasion, making it a promising target for therapeutic intervention. Additionally, the exploration of MALD1's structure and function can provide insights into its mechanisms of action, revealing new aspects of cellular machinery and signaling networks. Researchers are increasingly interested in the recombinant expression of MALD1 to facilitate detailed functional studies, including the assessment of post-translational modifications and protein-protein interactions. Understanding the role of MALD1 in health and disease could pave the way for innovative strategies in drug development and personalized medicine. This growing body of research underscores the importance of MALD1 as a biomarker and therapeutic target, highlighting the need for continued investigation into its multifaceted roles within cellular contexts.

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