Cat: PA2000-1009

Recombinant Human RVT Protein,His

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Analytical Data

  • Gene name

    RVT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RVT;Endogenous retrovirus group K member 19 Pol Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9WJR5

  • Expression Region

    1-959aa

  • AA Sequence

    NKSKKRRNRVSFLGAATVEPPKPIPLTWKTEKPVWVNQWPLPKQKLEALHLLANEQLEKGHIEPSFSPWNSPVFVIQKKSGKWRMLTDLRAVNAVNAVIQPMGPLQPGLPSLAMIPKDWPLIIIDLKDCFFTIPLAEQDCEKFAFTIPAINNKEPATRFQWKVLPQGMLNSPTICQTFVGRALQPVREKFSDCYIIHYIDDILCAAEMKDKLIDCYTFLQAEVANAGLAIASDKIQTSTPFHYLEMQIENRKIKPPKIEIRKDTLKTLNDFQKLLGDINWIRPTLGIPTYAMSNLFSILRGDSDLNSKRMLTPEATKEIKLVEEKIQSAQINRIDPLAPLQLLIFATAHSPTGIIIQNTDLVEWSFLPHSTVKTFTLYLDQMATLIGQTRLRIIKLCGNDPDKIVVPLTKEQVRQAFINSGAWQIGLANFVGIIDNHYPKTKIFQFLKMTTWILPKITRREPLENALTVFTDGSSNGKAAYTGPKERVIKTQYQSAQRAELVAVITVLQDFDQPINIISDSAYVVQATRDVETALIKYSMDDQLNQLFNLLQQTVRKRNFPFYITHIRAHTNLPGPLTKANEQADLLVSSALIKAQELHALTHVNVAGLKNKFDVTWKQAKDIVQHCTQCQVLHLPTQEAGVNPRGLCPNALWQMDVTHVSSFGRLSYIHVTVDTYSHFIWATCQTGESTSHVKKHLLSCFAVMGVPEKIKTDNGPGYCSKAFQKFLSQWKISHTTGIPYNSQGQAIVERTNRTLKTQLVKQKEGGDSKECTTPQMQLNLALYTLNFLNIYRNQTTTSAEQHLTGKKNSPHEGKLIWWKDNKNKTWEIGKVITWGRGFACVSPGENQLPVWIPTRHLKFYNEPIGDAKKSTSAETETPQSSTVDSQDEQNGDVRRTDEVAIHQESRAADLGTTKEADAVSYKISREHKGDTNPREYAACGLDDCINGGKSPYACRSSCS

  • Molecular Weight

    108.1 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

RVT (Recombinant Virus-like Protein) is an emerging area of research in biotechnology and virology, focusing on the development of recombinant proteins that mimic the structure and function of viral components without containing infectious material. The background of RVT research is rooted in the need for safer and more effective vaccines and therapeutics. Traditional vaccine development often relies on live attenuated or inactivated viruses, which can pose safety risks or have limitations in efficacy. Recombinant protein technology addresses these concerns by allowing for the production of non-infectious viral-like particles (VLPs) that can effectively stimulate immune responses. The ability to engineer RVT proteins for various applications, including vaccine development, diagnostics, and as therapeutic agents, has gained significant attention. These proteins can be produced in various expression systems, such as yeast, bacteria, or mammalian cells, making them versatile and efficient. Additionally, RVT research is advancing our understanding of viral mechanisms and interactions with the host immune system, offering insights that could lead to novel antiviral strategies. As ongoing studies continue to explore the potential of RVT in combatting viral diseases, including emerging and re-emerging infections, the overall landscape of vaccine and therapeutic options may be significantly enhanced, showcasing the importance of this research field in public health and infectious disease management.

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