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Search results for: 'recombinant'
ELISA, SDS-PAGE, WB
>95% as determined by SDS-PAGE.
16.68 kDa
1 mg, 50 μg, 100 μgELISA, SDS-PAGE, WB
>90% as determined by SDS-PAGE.
78.32 kDa
1 mg, 50 μg, 100 μgELISA, SDS-PAGE, WB
>95% as determined by SDS-PAGE.
24.40 kDa
1 mg, 50 μg, 100 μg- Human VSNL1 [orb2995179]
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 21 KDa. Observed: 32 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Predicted: 16.2 kDa. Observed: 15 kDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg- Featured
ActiveFeatured
ActiveGreater than 94.5% as determined by SDS-PAGE.
46.5 kDa
Mammalian cell
100 μg, 20 μg, 1 mg - Featured
Featured
≥95% as determined by SDS-PAGE
17 kDa
100 μg, 500 μg, 20 μg - 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 36.3 kDa after removal of the signal peptide.The apparent molecular mass of hFc-TGFBR1 is approximately 40-53 kDa due to glycosylation.
Mammalian
50 μg, 100 μg, 10 μg - 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 29.0 kDa after removal of the signal peptide. The apparent molecular mass of GRP-hFc is approximately 25-35 kDa due to glycosylation.
Mammalian
10 μg, 100 μg, 50 μg - 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 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









