Cat: PA2000-3688

Recombinant E.coli ribA Protein,His

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Analytical Data

  • Gene name

    ribA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ribA;GTP cyclohydrolase-2

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A7I7

  • Expression Region

    1-196aa

  • AA Sequence

    MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK

  • Molecular Weight

    25.8 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

The study of the speF recombinant protein is rooted in its crucial role in the biosynthesis of polyamines, particularly spermidine and spermine, which are vital for cellular growth and function. SpeF, or S-adenosylmethionine decarboxylase, is an enzyme that catalyzes the decarboxylation of S-adenosylmethionine to produce decarboxylated S-adenosylmethionine, a key intermediate in polyamine synthesis. Polyamines are known to be involved in various cellular processes, including DNA stabilization, protein synthesis, and cell proliferation. Mutations or dysregulation of speF have been linked to multiple pathological conditions, including cancer and neurodegenerative diseases, highlighting the enzyme's potential as a therapeutic target. The production of recombinant speF protein enables researchers to further investigate its enzymatic properties, functions, and interactions within cellular pathways. Understanding the molecular mechanisms by which speF influences polyamine metabolism can provide insights into its role in health and disease, making it a significant focus for biochemical and pharmacological studies.

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