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  • Unconjugated

    SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 14.2 KDa. Observed: 16 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • Unconjugated

    SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.. SEC-HPLC: Greater than 90% as determined by SEC-HPLC.(QC verified)

    Predicted: 15.1 KDa. Observed: 16-18 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • Unconjugated

    SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 13 KDa. Observed: 18 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • Unconjugated

    SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.. SEC-HPLC: Greater than 85% as determined by SEC-HPLC.(QC verified)

    Predicted: 23.27 KDa. Observed: 25-30 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • ActiveActive

    Unconjugated

    90%

    20.3 kDa

    20 μg, 50 μg
  • ActiveActive

    Unconjugated

    95%

    84.1 kDa

    100 μg, 1 mg
  • FeaturedFeatured Product

    Unconjugated

    The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 14.8 kDa after removal of the signal peptide.

    Mammalian

    50 μg, 100 μg, 10 μg
  • FeaturedFeatured Product
    ActiveActive

    > 96 % by SDS-PAGE and HPLC analyses.

    Approximately 11.5 kDa, a single non-glycosylated polypeptide chain containing 98 amino acids.

    Escherichia coli

    5 μg, 100 μg, 500 μg
  • SDS-PAGE

    Unconjugated

    > 85% as determined by SDS-PAGE

    0.5 mg, 1 mg, 0.1 mg
  • 152 kDa

    Human

    20 μg

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