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Search results for: 'yeast'
Featured
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- 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 20.7 kDa in SDS-PAGE under reducing conditions.
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 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
500 μg, 10 μg, 100 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 - Item 1 of 2Yeast cagA protein [orb246088]Featured
Greater than 90% as determined by SDS-PAGE.
35.5 kDa
Yeast
1 mg, 100 μg, 20 μg - Item 1 of 1Yeast ATG1 protein [orb418765]Featured
Greater than 90% as determined by SDS-PAGE.
50.4 kDa
E.coli
20 μg, 100 μg, 1 mg
