Cat: PA2000-4250

Recombinant E.coli R70M Protein,His

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Analytical Data

  • Gene name

    R70M

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    R70M;

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q50927

  • Expression Region

    27-198aa

  • AA Sequence

    AGVAEFNDKGELLLPKNYREWVMVGTQVTPNELNDGKAPFTEIMTVYVDPESYAHWKKTGEFRDGTVTVKELVSVGDRKGPGSGNGYFMGDYIGLEASVKDSQRFANEPGNWAFYIFYVPDTPLVAAAKNLPTAECAACHKENAKTDMVFTQFYPVLRAAKATGESGVVAPK

  • Molecular Weight

    34.7 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.

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Protein Description

The R70M recombinant protein has emerged as a significant focus of research due to its potential implications in various biomedical applications, particularly in the fields of enzyme technology and therapeutic development. This protein variant is characterized by a mutation at the 70th residue, where arginine is replaced by methionine (R70M), which may alter its functional properties and stability compared to the wild-type counterpart. Studies have indicated that such modifications can enhance the protein’s catalytic efficiency or alter its interaction with substrates, making it a valuable subject for protein engineering. Furthermore, understanding the structural and functional consequences of the R70M mutation can provide insights into disease mechanisms, particularly in conditions where enzyme dysfunction is implicated. The exploration of R70M also contributes to the broader field of synthetic biology, where engineered proteins can be designed for specific industrial processes or therapeutic applications. Researchers are actively investigating its properties through a combination of experimental and computational approaches, aiming to elucidate the relationship between its structure and function. This research avenue not only enhances our fundamental understanding of protein behavior but also opens up possibilities for innovative solutions to pressing medical and industrial challenges, positioning R70M as a promising candidate for future studies in protein biochemistry and biotechnology.

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