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Search results for: 'IL-9'

Items 1 - 10 of 65

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  • Featured
    Active

    > 95% as determined by SDS-PAGE and HPLC.

    14.1 kDa

    E.Coli

    10 μg, 100 μg, 500 μg
  • Featured
    Active

    > 97% as determined by SDS-PAGE and HPLC.

    14.2 kDa

    E.Coli

    100 μg, 500 μg, 10 μg
  • Active

    Unconjugated

    90%

    16.0 kDa

    100 μg, 1 mg
  • 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 40.0 kDa after removal of the signal peptide.

    Mammalian

    50 μg, 10 μg, 100 μg
  • 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 40.3 kDa after removal of the signal peptide. The apparent molecular mass of IL9-hFc is approximately 35-70 kDa due to glycosylation.

    Mammalian

    50 μg, 100 μg, 10 μg
  • Featured

    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 14.9 kDa after removal of the signal peptide. The apparent molecular mass of IL9-His is approximately 25-55 kDa due to glycosylation.

    Mammalian

    50 μg, 100 μg, 10 μg
  • Featured

    Greater than 85% as determined by SDS-PAGE.

    27.1 kDa

    E.coli

    100 μg, 1 mg, 20 μg
  • Greater than 95% as determined by reducing SDS-PAGE.

    Predicted: 15.16 KDa. Observed: 25-40 KDa, reducing conditions

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

    Predicted: 15.2 KDa. Observed: 28-42 KDa, reducing conditions

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

    >85%

    Synthetic

    1 mg, 5 mg

Items 1 - 10 of 65

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