Cat: IPD-X26902

Recombinant Human HSP90AA1 Protein (Baculovirus),His

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Analytical Data

  • Gene name

    HSP90AA1

  • 简介

    The HSP90AA1 protein is an important molecular chaperone that coordinates the maturation and regulation of specific target proteins critical for cell cycle control and signal transduction. Its ATPase activity drives a functional cycle that induces conformational changes in client proteins for activation. HSP90AA1 Protein, Human (sf9, His) is the recombinant human-derived HSP90AA1 protein, expressed by Sf9 insect cells, with N-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HSP90AA1; HSP90A; HSPCAHeat shock protein HSP 90-alpha

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P07900-1

  • Expression Region

    M1-D732

  • AA Sequence

    MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD

  • Protein Length

    Full Length of Isoform-1

  • Molecular Weight

    79.81 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

HSP90AA1, a member of the heat shock protein 90 (HSP90) family, plays a critical role in protein folding, stabilization, and the regulation of various cellular processes, including signal transduction, cell cycle progression, and response to stress. As a molecular chaperone, HSP90AA1 is involved in the maturation of numerous client proteins, many of which are key players in cancer development and progression. Overexpression of HSP90AA1 has been linked to tumorigenesis and resistance to therapy, making it a promising target for cancer treatment. Research into recombinant HSP90AA1 is vital for understanding its structure and function, as well as for the development of HSP90 inhibitors that can disrupt its activity. Recombinant protein production allows for detailed studies of HSP90AA1's role in cellular mechanisms and provides a basis for the design of therapeutic agents that can interfere with its interactions with oncogenic client proteins. Furthermore, characterizing recombinant HSP90AA1 can facilitate investigations into its post-translational modifications and interactions with co-chaperones, enhancing our comprehension of its complex regulatory networks. Overall, the study of recombinant HSP90AA1 is essential for elucidating its biological functions and therapeutic potential in treating various diseases, particularly cancer.

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