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Search results for: 'IL-1'

Items 81 - 90 of 691

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  • Featured

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

    16.9 KDa

    Mammalian

    10 μg, 50 μg
  • Featured

    >95% as determined by Tris-Bis PAGE; >95% as determined by SEC-HPLC

    Due to glycosylation, the protein migrates to 19 kDa based on Tris-Bis PAGE result.

    100 μg, 50 μg
  • Featured

    >95% as determined by SDS-PAGE

    25 kDa

    100 μg, 500 μg, 20 μg
  • Featured

    Greater than 85% as determined by SDS-PAGE.

    22.2 kDa

    E.coli

    20 μg, 100 μg, 1 mg
  • Featured

    Greater than 85% as determined by SDS-PAGE.

    87.9 kDa

    E.coli

    1 mg, 20 μg, 100 μg
  • Featured

    Greater than 90% as determined by SDS-PAGE.

    62.0 kDa

    E.coli

    20 μg, 100 μg, 1 mg
  • Featured

    Greater than 95% as determined by SDS-PAGE.

    24.9 kDa

    E.coli

    20 μg, 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 44.3 kDa after removal of the signal peptide. The apparent molecular mass of IL1A-mFc is approximately 35-70 kDa due to glycosylation.

    Mammalian

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

    Predicted: 17.1 KDa. Observed: 17 KDa, reducing conditions

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

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

    1 mg, 500 μg, 50 μg, 10 μg

Items 81 - 90 of 691

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