You have no items in your shopping cart.
Search results for: 'stem cell'
- Featured
ActiveFeatured
Active> 95 % by SDS-PAGE and 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 14.4-20 kDa in SDS-PAGE under reducing conditions.
Yeast
10 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 95 % by SDS-PAGE.
Approximately 28.8 kDa, a disulfide-linked homodimeric protein containing two 126 amino acid residues polypeptide. But it migrates with an apparent molecular mass of 33.6 kDa in SDS-PAGE.
Escherichia coli
10 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 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 - Featured
ActiveFeatured
Active> 95 % by SDS-PAGE analyses.
Approximately 7.5 kDa, a single non-glycosylated polypeptide chain containing 67 amino acids.
Escherichia coli
100 μg, 500 μg - Featured
ActiveFeatured
Active> 96 % by SDS-PAGE and HPLC analyses.
Approximately 28.6 kDa, a single non-glycosylated polypeptide chain containing 252 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 95 % by SDS-PAGE and HPLC analyses.
Approximately 9.6 kDa, a single non-glycosylated polypeptide chain containing 86 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 95 % by SDS-PAGE and HPLC analyses.
Approximately 18.5 kDa, a single non-glycosylated polypeptide chain containing 165 amino acids.
Escherichia coli
10 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 97 % by SDS-PAGE and 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 approximately 40 kDa in SDS-PAGE under non-reducing conditions.
Yeast
10 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 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 20.7 kDa in SDS-PAGE under reducing conditions.
Yeast
10 μg, 100 μg, 500 μg - Featured
ActiveFeatured
Active> 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
