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Search results for: 'recombinant'

Items 41 - 50 of 117085

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  • ELISA,  SDS-PAGE,  WB

    >95% as determined by SDS-PAGE.

    16.68 kDa

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

    >90% as determined by SDS-PAGE.

    78.32 kDa

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

    >95% as determined by SDS-PAGE.

    24.40 kDa

    1 mg, 50 μg, 100 μg
  • Unconjugated

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

    Predicted: 21 KDa. Observed: 32 KDa, reducing conditions

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

    Predicted: 16.2 kDa. Observed: 15 kDa, reducing conditions

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

    Greater than 94.5% as determined by SDS-PAGE.

    46.5 kDa

    Mammalian cell

    100 μg, 20 μg, 1 mg
  • ≥95% as determined by SDS-PAGE

    17 kDa

    100 μg, 500 μg, 20 μg
  • 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 36.3 kDa after removal of the signal peptide.The apparent molecular mass of hFc-TGFBR1 is approximately 40-53 kDa due to glycosylation.

    Mammalian

    50 μg, 100 μg, 10 μg
  • 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 29.0 kDa after removal of the signal peptide. The apparent molecular mass of GRP-hFc is approximately 25-35 kDa due to glycosylation.

    Mammalian

    10 μg, 100 μg, 50 μg
  • 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 43.5 kDa after removal of the signal peptide.The apparent molecular mass of IL1B-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    10 μg, 100 μg, 50 μg

Items 41 - 50 of 117085

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