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Search results for: 'IL-22'

Items 11 - 20 of 128

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  • Unconjugated

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

    Predicted: 43.4 KDa. Observed: 50-75 KDa, reducing conditions

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

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

    Predicted: 43.4 KDa. Observed: 50-62 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 95% as determined by SEC-HPLC. (Regularly tested)

    Predicted: 16.7 KDa. Observed: 15 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg
  • 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 33.9 kDa after removal of the signal peptide. The apparent molecular mass of IL22-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    10 μg, 100 μg, 50 μg
  • >90% as determined by SDS-PAGE

    17.8 kDa

    100 μg, 500 μg, 20 μg
  • ELISA,  WB

    >90% as determined by SDS-PAGE.

    18.6 kDa

    HEK293 cells

    0.05 mg
  • ELISA,  WB

    >95% by SDS PAGE analysis

    5 μg
  • Unconjugated

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

    51.8 KDa

    Mammalian

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

    Predicted: 51.8 KDa. Observed: 80-100 KDa, reducing conditions

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

    Predicted: 25.7 KDa. Observed: 44 KDa, reducing conditions

    10 μg, 50 μg, 500 μg, 1 mg

Items 11 - 20 of 128

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