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On Promotion
Category
Tested Applications
Conjugation
Biologically Active
Featured Product
Search results for: 'CXCL10'
- Featured
Active
Item 1 of 1FeaturedActive> 95 % by SDS-PAGE and HPLC analyses.
Approximately 8.7 kDa, a single non-glycosylated polypeptide chain containing 77 amino acids.
Escherichia coli
5 μg, 100 μg, 500 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 8.7 kDa, a single non-glycosylated polypeptide chain containing 77 amino acids.
Escherichia coli
100 μg, 500 μg, 5 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 8.7 kDa, a single non-glycosylated polypeptide chain containing 77 amino acids.
Escherichia coli
5 μg, 500 μg, 100 μg - FeaturedActiveItem 1 of 1FeaturedActive
> 97 % by SDS-PAGE and HPLC analyses.
Approximately 8.6 kDa, a single non-glycosylated polypeptide chain containing 77 amino acids.
Escherichia coli
500 μg, 5 μg, 100 μg - Item 1 of 1
- Item 1 of 1
- FeaturedItem 1 of 1Human CXCL10 Protein, hFc Tag [orb2321426]Featured
Unconjugated
The purity of the protein is greater than 90% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 34.8 kDa after removal of the signal peptide.
Mammalian
100 μg, 50 μg, 10 μg - FeaturedItem 1 of 1Cynomolgus CXCL10 Protein, hFc Tag [orb1173710]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 34.8 kDa after removal of the signal peptide.The apparent molecular mass of cCXCL10-hFc is approximately 25-55 kDa due to glycosylation.
Mammalian
10 μg, 100 μg, 50 μg 
Recombinant Human CXCL10 Protein [orb3002373]SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 8.6 KDa. Observed: 13 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg- Recombinant Human CXCL10 Protein [orb3002304]
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 36.6 KDa. Observed: 35 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mg
