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Search results for: 'TNF-alpha'
- ActiveActive
ELISA, SDS-PAGE
Unconjugated
>95% as determined by SDS-PAGE and SEC-MALS.
17.4 kDa
100 μg, 1 mg, 20 μg - ActiveActive
Unconjugated
>95% as determined by SDS-PAGE and SEC-MALS.
18.3 kDa
100 μg, 1 mg - Featured
ActiveFeatured
ActiveGreater than 90% as determined by SDS-PAGE.
19.4 kDa
Yeast
1 mg, 20 μg, 100 μg Unconjugated
SDS-PAGE: Greater than 85% as determined by reducing SDS-PAGE.
Predicted: 46.5 KDa. Observed: 55-60 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 20.39 KDa. Observed: 24-28 KDa, reducing conditions
50 μg, 10 μg, 500 μg, 1 mg- ActiveActive
Unconjugated
90%
18.6 kDa
100 μg, 1 mg - ActiveActive
Unconjugated
95%
19.1 kDa
100 μg, 1 mg - Featured
Featured
Unconjugated
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 18.1 kDa after removal of the signal peptide.
Mammalian
10 μg, 100 μg, 50 μg Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 19 KDa. Observed: 33-41 KDa, reducing conditions
1 mg, 10 μg, 50 μg, 500 μgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 51.9 KDa. Observed: 60-90 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg






