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> 95 % by SDS-PAGE and 90% by SEC-HPLC analyses.
Theoretically as a disulfide-linked homodimeric protein, the product consists of two 165 amino acid polypeptide chains. As a result of glycosylation, it migrates to at least two bands with molecular weights ranging from 25.7 kDa in SDS-PAGE under reducing conditions.
Yeast
10 μg, 100 μg, 500 μg- FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Theoretically as a disulfide-linked homodimeric protein, the product consists of two 166 amino acid polypeptide chains. As a result of glycosylation, it migrates to at least three bands with molecular weights ranging from 20-31 kDa in SDS-PAGE under reducing conditions.
Yeast
10 μg, 100 μg, 500 μg - Recombinant Human Interferon-alpha2c, Yeast [orb1906249]FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 19.3 kDa, a single polypeptide chain containing 165 amino acids.
Yeast
10 μg, 100 μg, 500 μg - FeaturedActive
> 95 % by SDS-PAGE and 90% by SEC-HPLC analyses.
Theoretically as a disulfide-linked homodimeric protein, the product consists of two 121 amino acid polypeptide chains. As a result of glycosylation, it migrates to at least two bands with molecular weights ranging from 18.5 kDa in SDS-PAGE under reducing conditions.
Yeast
500 μg, 10 μg, 100 μg - Human IL-11 [orb3002458]
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 19 KDa. Observed: 19 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg - Carassius auratus Leptin [orb3002239]
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 18.3 KDa. Observed: 17 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg