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Category
Tested Applications
Reactivity
Predicted Reactivity
Conjugation
Biologically Active
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Search results for: 'CD138'
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 51 KDa. Observed: 80-90 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgUnconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 25.2 KDa. Observed: 45-60 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgSDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Predicted: 51.1 KDa. Observed: 65-110 KDa, reducing conditions
1 mg, 500 μg, 50 μg, 10 μg- Featured
Item 1 of 3FeaturedELISA, WB
>90% as determined by SDS-PAGE.
27.5 kDa
HEK293 cells
0.025 mg - FeaturedItem 1 of 3Featured
ELISA, WB
>95% as determined by SDS-PAGE.
50.3 kDa
HEK293 cells
0.1 mg - FeaturedItem 1 of 1Featured
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 50.8 kDa after removal of the signal peptide. The apparent molecular mass of CD138-hFc-His is approximately 70-100 kDa due to glycosylation.
Mammalian
10 μg, 100 μg, 50 μg - FeaturedItem 1 of 1Featured
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 50.3 kDa after removal of the signal peptide.The apparent molecular mass of mCD138-hFc is approximately 55-70 kDa due to glycosylation.
Mammalian
100 μg, 10 μg, 50 μg - FeaturedItem 1 of 1Featured
Greater than 90% as determined by SDS-PAGE.
26.5 kDa
Yeast
1 mg, 20 μg, 100 μg - FeaturedItem 1 of 1Featured
Greater than 90% as determined by SDS-PAGE.
39.9 kDa
E.coli
100 μg, 1 mg, 20 μg
