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Search results for: 'proteins'

Items 1321 - 1330 of 105656

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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 39.4 kDa after removal of the signal peptide. The apparent molecular mass of RNF43-hFc is approximately 40-70 kDa due to glycosylation.

    Mammalian

    10 μg, 50 μg, 100 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 58.8 kDa after removal of the signal peptide. The apparent molecular mass of hFc-SPARC is approximately 55-70 kDa due to glycosylation.

    Mammalian

    10 μg, 50 μg, 100 μg
  • Featured

    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 77.2 kDa after removal of the signal peptide. The apparent molecular mass of MMP9(20-707)-His is approximately 70-100 kDa due to glycosylation.

    Mammalian

    50 μg, 10 μg, 100 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 43.9 kDa after removal of the signal peptide. The apparent molecular mass of EMCN-hFc is approximately 55-100 kDa due to glycosylation.

    Mammalian

    100 μg, 10 μg, 50 μg
  • Featured

    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 16.2 kDa after removal of the signal peptide. The apparent molecular mass of CLEC2D-His is approximately 15-25 kDa due to glycosylation.

    Mammalian

    10 μg, 50 μg, 100 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 37.7 kDa after removal of the signal peptide. The apparent molecular mass of CD63-His is approximately 35-55 kDa due to glycosylation.

    Mammalian

    50 μg, 10 μg, 100 μg
  • Featured

    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 57.2 kDa after removal of the signal peptide. The apparent molecular mass of ADGRE2-His is approximately 70-100 kDa due to glycosylation.

    Mammalian

    10 μg, 50 μg, 100 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 42 kDa after removal of the signal peptide. The apparent molecular mass of IL31-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    50 μg, 10 μg, 100 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 39.6 kDa after removal of the signal peptide. The apparent molecular mass of MDK-hFc is approximately 35-55 kDa due to glycosylation.

    Mammalian

    10 μg, 50 μg, 100 μg
  • Featured

    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.

    The protein has a predicted molecular mass of 60.6 kDa after removal of the signal peptide. The apparent molecular mass of MUC18-His is approximately 70-100 kDa due to glycosylation.

    Mammalian

    10 μg, 100 μg, 50 μg

Items 1321 - 1330 of 105656

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