Cat: IPD-X39220

Recombinant Human AHCYL1 Protein,His

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Analytical Data

  • Gene name

    AHCYL1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    XPVKONA; IRBIT; DCAL; Putative adenosylhomocysteinase 2; S-Adenosylhomocysteine Hydrolase-Like 1; Inositol 1,4,5-Trisphosphate Receptor-Binding Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43865

  • Expression Region

    Ser281~Tyr530

  • Molecular Weight

    32kDa

  • 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

AHCYL1, or Adenosylhomocysteinase-Like 1, is a member of the adenosylhomocysteinase family, which plays a crucial role in the methionine cycle and sulfur amino acid metabolism. This enzyme is known to catalyze the hydrolysis of adenosylhomocysteine (AdoHcy) to produce homocysteine and adenosine, thereby participating in the regulation of cellular levels of these metabolites. The study of AHCYL1 has gained attention due to its potential implications in various physiological processes and diseases. Abnormalities in homocysteine metabolism are linked to cardiovascular diseases, neurodegenerative disorders, and other health issues, making AHCYL1 a potential target for therapeutic intervention. Furthermore, recent studies suggest that AHCYL1 may also play a role in cellular signaling pathways and stress responses. Understanding the structure, function, and regulation of AHCYL1, including the characterization of recombinant AHCYL1 protein, can provide insights into its biological significance and therapeutic potential. Research on AHCYL1 not only enhances our understanding of metabolic regulation but also opens avenues for developing new strategies for the treatment of diseases related to aberrant homocysteine levels.

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