Cat: PA1000-1051

Recombinant Human ESD Protein,His

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Analytical Data

  • Gene name

    ESD

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ESD;S-formylglutathione hydrolase

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10768

  • Expression Region

    1-282aa

  • AA Sequence

    MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA

  • 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

Electrostatic discharge (ESD)-related protein restructuring is a vital area of research, particularly as electronic devices proliferate and become increasingly compact. ESD events, resulting from the accumulation of static electricity, can lead to significant damage in sensitive electronic components, affecting their performance and reliability. In this context, researchers focus on understanding the molecular mechanisms underlying protein stabilization and restructuring in response to ESD. Proteins undergo conformational changes upon exposure to ESD, which can alter their functional properties and, consequently, the behavior of the devices they support. Investigating the effects of ESD on protein structure involves employing advanced techniques such as nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and mass spectrometry to elucidate these complex interactions at the molecular level. Insights gained from these studies can inform the development of ESD-resistant materials and protective coatings, enhancing the durability and lifespan of electronic components. Moreover, this research has broader implications for improving the design of various electronic devices, from smartphones to aerospace technology, where ESD resilience is critical. Understanding ESD-induced protein dynamics not only contributes to material science but also fosters innovation in nanotechnology and electronic engineering, aiming to create more robust systems against electrical disturbances in the future.

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