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On Promotion
Species Host
Predicted Reactivity
Conjugation
Clonality
Biologically Active
Featured Product
All Products
- Featured
Active
FeaturedActive> 95 % by SDS-PAGE.
Approximately 28.9 kDa, a single non-glycosylated polypeptide chain containing 264 amino acids.
Escherichia coli
1 mg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 7.5 kDa, a single non-glycosylated polypeptide chain containing 65 amino acids.
Escherichia coli
10 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 22.9 kDa, a single non-glycosylated polypeptide chain containing 200 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 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 - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 19.8 kDa, a single non-glycosylated polypeptide chain containing 181 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 20.0 kDa, a single non-glycosylated polypeptide chain containing 166 amino acids.
Escherichia coli
10 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 34.6 kDa, a disulfide-linked homodimer consisting of two 152 amino acid polypeptide chains.
Escherichia coli
500 μg, 5 μg, 100 μg - FeaturedActiveFeaturedActive
> 95% by SDS-PAGE analyses.
Approximately 6 kDa, a single non-glycosylated polypeptide chain containing 50 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - FeaturedActiveFeaturedActive
> 97 % by SDS-PAGE analyses.
Approximately 27 kDa, a disulfide-linked homodimer of two 117 amino acid, C-terminal polyhistidine tagged proteins.
Escherichia coli
10 μg, 100 μg - FeaturedActiveFeaturedActive
> 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