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Search results for: 'proteins'

Items 1111 - 1120 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 37.0 kDa after removal of the signal peptide. The apparent molecular mass of CDH17(567-667)-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 69.2 kDa after removal of the signal peptide. The apparent molecular mass of SEMA7A-His is approximately 70-100 kDa due to glycosylation.

    E.coli

    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 64.3 kDa after removal of the signal peptide. The apparent molecular mass of GPR64-His is approximately 100-250 kDa due to glycosylation.

    E.coli

    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 25.0 kDa after removal of the signal peptide. The apparent molecular mass of CRLF2-His is approximately 25-55 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 42.2 kDa after removal of the signal peptide. The apparent molecular mass of cCD7-hFc 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 86.0 kDa after removal of the signal peptide.

    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 46.9 kDa after removal of the signal peptide. The apparent molecular mass of LRP10-His is approximately 55-70 kDa due to glycosylation.

    E.coli

    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 50.3 kDa after removal of the signal peptide.

    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 34.9 kDa after removal of the signal peptide. The apparent molecular mass of CCL19-hFc is approximately 25-55 kDa due to glycosylation.

    E.coli

    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 53.5 kDa after removal of the signal peptide. The apparent molecular mass of ALPP-His is approximately 55-70 kDa due to glycosylation.

    E.coli

    10 μg, 50 μg, 100 μg

Items 1111 - 1120 of 105656

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