Cat: IPD-X41620

Recombinant Synechocystis sp. gltS Protein ,His & Myc

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Analytical Data

  • Gene name

    gltS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (FD-GOGAT)

  • Species

    Synechocystis sp.

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P55038

  • Expression Region

    1-435aa

  • Molecular Weight

    55.5 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 study of GLT (glutamate transporters) S recombinant proteins has gained significant attention due to the crucial role these transporters play in maintaining synaptic glutamate levels and overall neurotransmitter balance in the central nervous system. GLT-1, in particular, is the predominant glutamate transporter in the brain, responsible for the uptake of extracellular glutamate, thereby preventing excitotoxicity, which can lead to neurodegenerative diseases such as Alzheimer's, Parkinson's, and multiple sclerosis. Understanding the structural and functional characteristics of GLT-1 through recombinant protein studies provides valuable insights into its mechanism of action, regulation, and interaction with various ligands and inhibitors. Moreover, the development of recombinant GLT-1 proteins allows for high-throughput screening of potential therapeutic agents that can modulate glutamate transport, offering promising avenues for drug discovery aimed at protecting neurons from glutamate-induced toxicity. As researchers continue to explore the dynamics of GLT transporters, including their conformational states and interactions with other cellular components, the foundational knowledge gained may pave the way for innovative therapeutic strategies aimed at addressing excitotoxicity-related conditions, highlighting the significance of GLT-S recombinant protein research in modern neuroscience and pharmacology.

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