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On Promotion
Species Host
Predicted Reactivity
Conjugation
Clonality
Biologically Active
Featured Product
All Products
- Active
Active> 95 % by SDS-PAGE analyses.
Apparent molecular mass of 65 kDa, 43-45 kDa and 20 kDa in SDS-PAGE under reducing conditions.
Spodoptera frugiperda, Sf 21 (baculovirus)
10 μg, 100 μg - Featured
ActiveFeaturedActive> 95 % by SDS-PAGE and HPLC analyses.
Approximately 17.9 kDa, a single non-glycosylated polypeptide chain containing 153 amino acids.
Escherichia coli
500 μg, 10 μg, 100 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE analyses.
Apparent molecular mass of 45-50 kDa in SDS-PAGE under reducing conditions, a single glycosylated polypeptide protein consisting of 339 amino acids.
Spodoptera frugiperda, Sf21 (baculovirus).
10 μg, 100 μg - FeaturedActiveFeaturedActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 14.2 kDa, a single non-glycosylated polypeptide chain containing 127 amino acids.
Escherichia coli
500 μg, 5 μg, 100 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 5.2 kDa, a single non-glycosylated polypeptide chain containing 48 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 20.7 kDa, a disulfide-linked homodimer of two 96 amino acid polypeptide chains.
Escherichia coli
500 μg, 5 μg, 100 μg - FeaturedActiveFeaturedActive
> 95 % by SDS-PAGE and HPLC analyses.
Approximately 29.9 kDa, a homodimeric protein consisting of two 134 amino acid non-glycosylated polypeptide chains.
Escherichia coli
500 μg, 10 μg, 100 μg - FeaturedActiveFeaturedActive
> 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 - FeaturedActiveFeaturedActive
> 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 - FeaturedActiveFeaturedActive
> 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