Cat: PA1000-4944

Recombinant Human VCP Protein,His

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Analytical Data

  • Gene name

    VCP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    VCP;Small VCP/p97-interacting Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P55072

  • Expression Region

    1-806aa

  • AA Sequence

    MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQ LFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVI SIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGD IFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNE VGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTG KTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRP NSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVA NETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMD DFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHP DKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTM WFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRV INQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDE KSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIR ESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDN DIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDN DDDLYG

  • Molecular Weight

    116 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

VCP (Valosin-containing protein), also known as p97, is a member of the AAA ATPase family and plays a critical role in various cellular processes, including protein degradation, membrane fusion, and cell cycle regulation. Dysfunction of VCP is associated with multiple human diseases, including frontotemporal dementia, inclusion body myopathy, and amyotrophic lateral sclerosis (ALS). Given its significant implications in these pathologies, the study of VCP has garnered considerable attention in the fields of molecular biology and biochemistry. Researchers have focused on understanding its structure-function relationship and the mechanisms by which VCP interacts with various substrates and cofactors. The production of recombinant VCP proteins through techniques such as bacterial or mammalian cell expression systems has become essential for these studies, enabling scientists to investigate its biochemical properties and regulatory mechanisms in a controlled environment. This research is pivotal not only for elucidating the normal physiological roles of VCP but also for developing potential therapeutic strategies targeting its dysfunction in disease contexts. Furthermore, recombinant VCP proteins can serve as valuable tools in drug discovery and the screening of small molecules that may modulate its activity, presenting new avenues for treatment options in VCP-related diseases. Overall, the investigation of VCP and its recombinant forms represents a promising frontier in understanding key cellular processes and addressing the challenges posed by neurodegenerative conditions linked to its malfunction.

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