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Search results for: 'IL-23'

Items 11 - 20 of 106

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  • Featured

    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 44.8 and 35.5 kDa after removal of the signal peptide. The apparent molecular mass of IL23A-hFc and IL12B-His is approximately 35-55 kDa due to glycosylation.

    E.coli

    10 μg, 50 μg, 100 μg
  • Featured

    The purity of the protein is greater than 90% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 45.8 kDa after removal of the signal peptide.

    Mammalian

    10 μg, 50 μg, 100 μg
  • Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 81.3 KDa. Observed: 80-110 KDa, reducing conditions

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

    Predicted: 19.7&35.8 KDa. Observed: 40&20 KDa, reducing conditions

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

    Predicted: 55.2 KDa. Observed: 60-90 KDa, reducing conditions

    1 mg, 500 μg, 50 μg, 10 μg
  • Greater than 90% as determined by reducing SDS-PAGE.

    Predicted: 67.4 KDa. Observed: 90-110 KDa, reducing conditions

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

    Predicted: 19.7&35.8 KDa. Observed: 18&40-55 KDa, reducing conditions

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

    Predicted: 19.7&36.8 KDa. Observed: 40-55&20 KDa, reducing conditions

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

    Predicted: 38.7 KDa. Observed: 50-90 KDa, reducing conditions

    1 mg, 500 μg, 50 μg, 10 μg
  • Greater than 90% as determined by reducing SDS-PAGE.

    Predicted: 65 KDa. Observed: 90-120 KDa, reducing conditions

    1 mg, 500 μg, 50 μg, 10 μg

Items 11 - 20 of 106

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