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On Promotion
Category
Tested Applications
Conjugation
Biologically Active
Featured Product
Search results for: 'CCL5'
- Featured
Active
Item 1 of 1FeaturedActive> 97% as determined by SDS-PAGE and HPLC.
7.9 kDa
E.Coli
5 μg, 100 μg, 500 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 98% as determined by SDS-PAGE and HPLC.
7.8 kDa
E.Coli
5 μg, 100 μg, 500 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 98 % by SDS-PAGE and HPLC analyses.
Approximately 7.8 kDa, a single non-glycosylated polypeptide chain containing 68 amino acids.
Escherichia coli
100 μg, 500 μg, 5 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 7.9 kDa, a single non-glycosylated polypeptide chain containing 68 amino acids.
Escherichia coli
100 μg, 500 μg, 5 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 98 % by SDS-PAGE and HPLC analyses.
Approximately 7.8 kDa, a single non-glycosylated polypeptide chain containing 68 amino acids.
Escherichia coli
500 μg, 5 μg, 100 μg - Item 1 of 1
10 kDa
Human
20 μg - FeaturedItem 1 of 1Human RANTES protein [orb222832]Featured
SDS-PAGE, WB
Unconjugated
> 85% as determined by SDS-PAGE
28 KDa
100 μg - Item 1 of 1
- FeaturedItem 1 of 1Featured
Greater than 90% as determined by SDS-PAGE.
14.8 kDa
E.coli
1 mg, 100 μg, 20 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 34.0 kDa after removal of the signal peptide. The apparent molecular mass of CCL5-hFc is approximately 35-55 kDa due to glycosylation.
Mammalian
10 μg, 50 μg, 100 μg
