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Search results for: 'IL-31'
SDS-PAGE: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Predicted: 57.5 KDa. Observed: 90-130 KDa, reducing conditions
1 mg, 500 μg, 50 μg, 10 μg- Featured
ActiveFeatured
Active> 97% as determined by SDS-PAGE and HPLC.
15.8 kDa
E.Coli
10 μg, 100 μg, 500 μg ELISA, SDS-PAGE, WB
>90% as determined by SDS-PAGE.
18.27 kDa
1 mg, 50 μg, 100 μgUnconjugated
SDS-PAGE: Greater than 90% as determined by reducing SDS-PAGE.
Predicted: 82.03 KDa. Observed: 132 KDa, reducing conditions
10 μg, 50 μg, 500 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 42 kDa after removal of the signal peptide. The apparent molecular mass of IL31-hFc is approximately 35-55 kDa due to glycosylation.
Mammalian
10 μg, 50 μg, 100 μg - ActiveActive
Unconjugated
95%
83.5 kDa
1 mg, 100 μg - ActiveActive
Unconjugated
95%
59.0 kDa
1 mg, 100 μg - Featured
Featured
Unconjugated
The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 17.2 kDa after removal of the signal peptide.
Mammalian
100 μg, 10 μg, 50 μg - Featured
Featured
Unconjugated
The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 16.2 kDa after removal of the signal peptide. The apparent molecular mass of fIL31-His is approximately 15-25 kDa due to glycosylation.
Mammalian
50 μg, 10 μg, 100 μg - Featured
Featured
Unconjugated
The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 16.5 kDa after removal of the signal peptide. The apparent molecular mass of dIL31-His is approximately 15-25 kDa due to glycosylation.
Mammalian
100 μg, 10 μg, 50 μg








