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Reactivity
Predicted Reactivity
Conjugation
Biologically Active
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Search results for: 'IL-1'
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 17.1 KDa. Observed: 17 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 17 KDa. Observed: 14-16 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 62.7 KDa. Observed: 90-110 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 36.6 KDa. Observed: 55-70 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 68 KDa. Observed: 80-100 KDa, reducing conditions
1 mg, 10 μg, 50 μg, 500 μgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 40 KDa. Observed: 50-60 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 17.27 KDa. Observed: 16 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg- Featured
Item 1 of 4FeaturedUnconjugated
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 43.5 kDa after removal of the signal peptide.The apparent molecular mass of IL1B-hFc is approximately 35-55 kDa due to glycosylation.
Mammalian
10 μg, 100 μg, 50 μg Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 39.9 KDa. Observed: 50-80 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 16.8 KDa. Observed: 17 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg
