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Search results for: 'IL-20'

Items 11 - 20 of 69

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  • 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 44.3 kDa after removal of the signal peptide. The apparent molecular mass of IL17B-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    100 μg, 10 μg, 50 μg
  • Unconjugated

    Greater than 85% as determined by reducing SDS-PAGE.

    49.6 KDa

    Mammalian

    10 μg, 50 μg
  • Unconjugated

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

    52.4 KDa

    Mammalian

    10 μg, 50 μg
  • SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 52.4 KDa. Observed: 70-85 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 26.3 KDa. Observed: 35-50 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 17.7 KDa. Observed: 17 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • ELISA,  SDS-PAGE,  WB

    >90% as determined by SDS-PAGE.

    18.84 kDa

    1 mg, 50 μg, 100 μg
  • ELISA,  SDS-PAGE,  WB

    >90% as determined by SDS-PAGE.

    20.45 kDa

    1 mg, 50 μg, 100 μg
  • ELISA,  SDS-PAGE,  WB

    >90% as determined by SDS-PAGE.

    30.8 kDa

    1 mg, 50 μg, 100 μg
  • ELISA,  SDS-PAGE,  WB

    >90% as determined by SDS-PAGE.

    23.60 kDa

    1 mg, 50 μg, 100 μg

Items 11 - 20 of 69

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