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Search results for: 'CCL2'

Items 11 - 20 of 90

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  • ELISA,  WB

    >95% by SDS PAGE analysis

    5 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 34.8 kDa after removal of the signal peptide. The apparent molecular mass of CCL2-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

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

    Predicted: 8.7 KDa. Observed: 13 KDa, reducing conditions

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

    Predicted: 8.5 KDa. Observed: 12 KDa, reducing conditions

    500 μg, 1 mg, 10 μg, 50 μg
  • ELISA,  WB

    >95% by SDS PAGE analysis

    5 μg
  • ELISA,  SDS-PAGE,  WB

    Unconjugated

    > 85%

    31.8 kDa

    0.5 mg, 100 μg
  • HPLC

    Unconjugated

    Synthesis

    1 mg
  • HPLC

    Unconjugated

    Synthesis

    1 mg
  • >90% as determined by SDS-PAGE

    15/18 kDa

    20 μg, 100 μg, 500 μg
  • ELISA,  SDS-PAGE,  WB

    >90% as determined by SDS-PAGE.

    16.75 kDa

    1 mg, 50 μg, 100 μg

Items 11 - 20 of 90

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