Cat: PA2000-7293

Recombinant Human EFS Protein,GST

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Analytical Data

  • Gene name

    EFS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    EFS; CASS3Embryonal Fyn-associated substrate; hEFS; Cas scaffolding protein family member 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43281

  • Expression Region

    1-561aa

  • AA Sequence

    MAIATSTQLA RALYDNTAES PQELSFRRGD VLRVLQREGA GGLDGWCLCS LHGQQGIVPA NRVKLLPAGP APKPSLSPAS PAQPGSPYPA PDHSNEDQEV YVVPPPARPC PTSGPPAGPC PPSPDLIYKI PRASGTQLAA PRDALEVYDV PPTALRVPSS GPYDCPASFS HPLTRVAPQP PGEDDAPYDV PLTPKPPAEL EPDLEWEGGR EPGPPIYAAP SNLKRASALL NLYEAPEELL ADGEGGGTDE GIYDVPLLGP EAPPSPEPPG ALASHDQDTL AQLLARSPPP PHRPRLPSAE SLSRRPLPAL PVPEAPSPSP VPSPAPGRKG SIQDRPLPPP PPRLPGYGGP KVEGDPEGRE MEDDPAGHHN EYEGIPMAEE YDYVHLKGMD KAQGSRPPDQ ACTGDPELPE RGMPAPQEAL SPGEPLVVST GDLQLLYFYA GQCQSHYSAL QAAVAALMSS TQANQPPRLF VPHSKRVVVA AHRLVFVGDT LGRLAASAPL RAQVRAAGTA LGQALRATVL AVKGAALGYP SSPAIQEMVQ CVTELAGQAL QFTTLLTSLA P

  • Molecular Weight

    58.8 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

EFS (Eukaryotic Translation Initiation Factor 2 Alpha Subunit Kinase 3) is a critical regulator of cellular stress responses, particularly in the context of translation initiation and apoptosis. Research on EFS fusion proteins has gained considerable attention due to their implications in various diseases, including cancer and neurodegenerative disorders. These proteins play a pivotal role in modulating the global protein synthesis machinery under stress conditions by phosphorylating the eIF2α subunit of the translation initiation factor, thereby affecting the rate of protein synthesis and the selective translation of specific mRNAs. Understanding the molecular mechanisms of EFS and its associated pathways can provide insights into how cells adapt to stress and maintain homeostasis. Furthermore, studies have shown that aberrations in EFS function can lead to maladaptive responses, contributing to the pathogenesis of several conditions. Therefore, the development of recombinant EFS proteins offers a promising avenue for probing their biological roles and potential therapeutic applications. Researchers are focusing on the structural and functional characterization of EFS, along with its interaction partners, to elucidate its contribution to stress response pathways and evaluate its potential as a drug target. This growing body of work emphasizes the need for advanced methodologies in producing and analyzing EFS proteins, highlighting a significant area of exploration for future biopharmaceutical development and therapeutic interventions. Overall, the comprehensive study of EFS fusion proteins can enhance our understanding of their multifaceted roles in cellular processes and pave the way for innovative strategies in treating diseases linked to translation regulation.

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