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  • Unconjugated

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

    Predicted: 14.9 kDa. Observed: 27-37 kDa, reducing conditions

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

    > 96% as determined by SDS-PAGE and HPLC.

    8.7 kDa

    E.Coli

    100 μg, 5 μg, 500 μg
  • FeaturedFeatured Product
    ActiveActive

    > 96 % by SDS-PAGE and HPLC analyses.

    Approximately 8.7 kDa, a single non-glycosylated polypeptide chain containing 76 amino acids.

    Escherichia coli

    500 μg, 5 μg, 100 μg
  • 11 kDa

    Human

    20 μg
  • ELISA,  SDS-PAGE,  WB

    Unconjugated

    > 90%

    12.5 kDa

    0.5 mg, 1 mg
  • ELISA,  SDS-PAGE,  WB

    Unconjugated

    > 90%

    26.6 kDa

    0.5 mg, 1 mg
  • FeaturedFeatured Product

    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, 50 μg, 10 μg
  • 11 kDa

    Human

    100 μg
  • FeaturedFeatured Product

    >45% as determined by SDS-PAGE

    43 kDa

    100 μg, 500 μg, 20 μg
  • FeaturedFeatured Product

    >90% as determined by SDS-PAGE

    15/18 kDa

    500 μg, 100 μg, 20 μg

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