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Items 11 - 20 of 577

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  • Unconjugated

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

    Predicted: 16.8 KDa. Observed: 17 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: 17.3 KDa. Observed: 17 KDa, reducing conditions

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

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

    Predicted: 39.9 KDa. Observed: 50-80 KDa, reducing conditions

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

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

    Predicted: 17.27 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.

    Predicted: 68 KDa. Observed: 80-100 KDa, reducing conditions

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

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

    Predicted: 40 KDa. Observed: 50-60 KDa, reducing conditions

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

    SDS-PAGE: Greater than 90% as determined by reducing SDS-PAGE.

    Predicted: 43.4 KDa. Observed: 54 KDa, reducing conditions

    1 mg, 10 μg, 50 μg, 500 μg
  • 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 43.5 kDa after removal of the signal peptide.The apparent molecular mass of IL1B-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    50 μg, 100 μg, 10 μg
  • ActiveActive

    Unconjugated

    90%

    37.8 kDa

    100 μg, 1 mg
  • ActiveActive

    Unconjugated

    95%

    62.4 kDa

    100 μg, 1 mg

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