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Conjugation
Biologically Active
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Active> 96 % by SDS-PAGE and HPLC analyses.
Approximately 5.2 kDa, a single non-glycosylated polypeptide chain containing 45 amino acid residues.
100 μg, 500 μg - ActiveActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 16.6 kDa, a single non-glycosylated polypeptide chain containing 141 amino acid residues.
10 μg, 100 μg, 500 μg - ActiveActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 10.6 kDa, a single non-glycosylated polypeptide chain containing 91 amino acids
10 μg, 100 μg, 500 μg - ActiveActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 3.6 kDa, a single non-glycosylated polypeptide chain containing 35 amino acids.
500 μg, 100 μg, 10 μg - ActiveActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 5.8 kDa, a single non-glycosylated polypeptide chain containing 51 amino acids.
500 μg, 100 μg, 5 μg - ActiveActive
> 95 % by SDS-PAGE analyses.
Approximately 26.0 kDa, a homodimeric protein consisting of two 116 amino acid polypeptide chains.
10 μg, 100 μg, 500 μg - ActiveActive
> 95 % by SDS-PAGE analyses.
Apparent molecular mass of 24 kDa in SDS-PAGE under non-reducing conditions, 14 kDa under reducing conditions, a disulfide-linked homodimer of two 116 amino acid glycosylated polypeptide chains.
10 μg, 100 μg, 500 μg - ActiveActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 31.5 kDa, a single non-glycosylated polypeptide chain containing 288 amino acids.
500 μg, 5 μg, 100 μg - ActiveActive
> 98 % by SDS-PAGE and HPLC analyses.
Approximately 8.5 kDa, a single non-glycosylated polypeptide chain containing 76 amino acids.
100 μg, 500 μg - ActiveActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 22.9 kDa, a single non-glycosylated polypeptide chain containing 200 amino acids.
5 μg, 100 μg, 500 μg