Cat: PA2000-551DB

Recombinant Human FLNa Protein,His

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Analytical Data

  • Gene name

    FLNa

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FLNa;FLN;FLN1;Filamin-A

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96C61

  • Expression Region

    1-838aa

  • AA Sequence

    MPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFY VDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAE ISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMR MSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGI SFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHE GHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPT EPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSH CDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGT HTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEF SIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSV KFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNG AKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGT HIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGA GALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGG SPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASK VVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHV GSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP

  • Molecular Weight

    118 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

Filamin A (FLNa) is a crucial actin-binding protein that plays a significant role in the regulation of cellular structure and mechanical properties. It acts as a scaffold, linking various membrane proteins to the cytoskeleton, thereby influencing cell shape, motility, and signaling pathways. Mutations in the FLNa gene are associated with several human diseases, including congenital disorders, cardiomyopathies, and neurological conditions, underscoring its importance in maintaining cellular integrity and function. The study of FLNa recombinant proteins has emerged as a pivotal area of research, enabling scientists to dissect its structural and functional properties in detail. By expressing FLNa as a recombinant protein in various expression systems, researchers aim to investigate its interaction with actin filaments, as well as its role in ligand binding and signal transduction. Understanding these interactions at the molecular level can provide insights into the mechanistic underpinnings of diseases linked to FLNa dysfunction. Furthermore, FLNa recombinant proteins can serve as valuable tools in drug discovery and development, particularly in identifying compounds that target FLNa-related pathways. The ongoing research in this field has the potential to reveal novel therapeutic strategies, contributing to the treatment of conditions in which FLNa is implicated, while also advancing our overall knowledge of cytoskeletal dynamics and cellular mechanics. Thus, the investigation of FLNa recombinant proteins not only enhances our understanding of basic cell biology but also holds promise for clinical applications aimed at combating FLNa-related diseases.

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