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Search results for: 'CD86'

Items 1 - 10 of 105

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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 52.4 kDa after removal of the signal peptide.

    Mammalian

    100 μg, 10 μg, 50 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 51.5 kDa after removal of the signal peptide.

    Mammalian

    100 μg, 10 μg, 50 μg
  • Featured

    Greater than 95% as determined by SDS-PAGE.

    26.69 kDa

    Mammalian cell

    10 μg, 50 μg, 1 mg, 500 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 51.4 kDa after removal of the signal peptide. The apparent molecular mass of mB7-2-hFc is approximately 55-70 kDa due to glycosylation.

    Mammalian

    100 μg, 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 55-70 kDa based on Tris-Bis PAGE result.

    50 μg, 100 μg
  • Featured

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

    Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result.

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

    Predicted: 28.4 KDa. Observed: 55-80 KDa, reducing conditions

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

    Predicted: 52.2 KDa. Observed: 68-95 KDa, reducing conditions

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

    Predicted: 52.5 KDa. Observed: 70-100 KDa, reducing conditions

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

    Predicted: 25.9 KDa. Observed: 35-55 KDa, reducing conditions

    1 mg, 500 μg, 50 μg, 10 μg

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