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Your Position: Home > Other Recombinant Proteins > S100A1 > Human S100A1 Protein

Human S100A1 Protein

  • Synonym
    S100A1
  • Source
    Human S100A1, His Tag (S11-H5124) is expressed from E.coli cells. It contains AA Met 1 - Ser 94 (Accession # AAH14392).
    Predicted N-terminus: Met
  • Molecular Characterization
    S100A1(Met 1 - Ser 94) AAH14392

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 11.4 kDa. The protein migrates as 11 kDa under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH8.0. Normally trehalose is added as protectant before lyophilization.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    No activity loss is observed after storage at:

    1. 4-8°C for 12 months in lyophilized state;

    2. -70°C for 3 months under sterile conditions after reconstitution.

SDS-PAGE
Human S100A1, His Tag (Cat. No. S11-H5124) SDS-PAGE gel

Human S100A1, His Tag on SDS-PAGE  under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

  • Background
    Protein S100-A1 / S100A1 is a Ca2+binding protein of the EF-hand type that belongs to the S100 protein family. S100 proteins consisting of at least 19 members exist as dimers in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell-cycle progression and cell differentiation. S100-A1 can weakly bind calcium but bind zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites.
  • References
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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Price(USD) : $300.00

Price(USD) : $1980.00

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