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    Greater than 95% as determined by SDS-PAGE.

    15.9 kDa

    Baculovirus

    100 μg, 20 μg, 1 mg
  • Featured

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

    Due to glycosylation, the protein migrates to 35-42 kDa based on Tris-Bis PAGE result.

    100 μg
  • 25.1 kDa

    Mammalian cell

    20 μg, 1 mg, 100 μg
  • ELISA

    200 μl, 20 μl
  • Featured
    Active

    Greater than 95% as determined by SDS-PAGE

    22.8 kDa

    Yeast

    1 mg, 20 μg, 100 μg
  • Featured
    Active

    Greater than 95% as determined by SDS-PAGE.

    41.5 kDa

    Mammalian cell

    20 μg, 100 μg, 1 mg
  • Featured
    Active

    Greater than 95% as determined by SDS-PAGE.

    24.4 kDa

    Mammalian cell

    20 μg, 100 μg, 1 mg
  • Featured
    Active

    Greater than 90% as determined by SDS-PAGE.

    22.7 kDa

    Mammalian cell

    1 mg, 20 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 47.4 kDa after removal of the signal peptide. The apparent molecular mass of RHOB-hFc is approximately 35-55 kDa due to glycosylation.

    E.coli

    10 μg, 50 μg, 100 μg
  • SDS-PAGE

    Unconjugated

    Mouse IgG was prepared from normal mouse serum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer stated above. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Mouse IgG and anti-Mouse Serum.

    Mouse

    25 mg

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