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Search results for: 'CD86'
- Human B7-2 Protein, mFc-His Tag [orb689395]Featured
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 52.4 kDa after removal of the signal peptide.
Mammalian
100 μg, 10 μg, 50 μg - Human B7-2 Protein, hFc Tag [orb689458]Featured
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 51.5 kDa after removal of the signal peptide.
Mammalian
100 μg, 10 μg, 50 μg - Human CD86 protein [orb594870]Featured
Greater than 95% as determined by SDS-PAGE.
26.69 kDa
Mammalian cell
10 μg, 50 μg, 1 mg, 500 μg - Mouse B7-2 Protein, hFc Tag [orb1290895]Featured
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 51.4 kDa after removal of the signal peptide. The apparent molecular mass of mB7-2-hFc is approximately 55-70 kDa due to glycosylation.
Mammalian
100 μg, 10 μg, 50 μg - Featured
>95% as determined by Tris-Bis PAGE; >95% as determined by SEC-HPLC
Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result.
50 μg, 100 μg - Featured
>95% as determined by Tris-Bis PAGE; >95% as determined by SEC-HPLC
Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result.
20 μg, 100 μg - Biotinylated Human B7-2 (C-Avi-6His) [orb2993754]
Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 28.4 KDa. Observed: 55-80 KDa, reducing conditions
100 μg, 20 μg - Recombinant Mouse B7-2 (C-Fc) [orb2994404]
Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 52.2 KDa. Observed: 68-95 KDa, reducing conditions
1 mg, 500 μg, 50 μg, 10 μg - Recombinant Cynomolgus B7-2 (C-Fc) [orb2994271]
Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 52.5 KDa. Observed: 70-100 KDa, reducing conditions
1 mg, 500 μg, 50 μg, 10 μg - Recombinant Rat CD86 (C-6His) [orb2994288]
Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 25.9 KDa. Observed: 35-55 KDa, reducing conditions
1 mg, 500 μg, 50 μg, 10 μg