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Description
Research Area
Images & Validation
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| Application Notes |
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Key Properties
−| Source | Sf9, Baculovirus cells |
|---|---|
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Protein Sequence | YFNETADLPC QFANSQNQSL SELVVFWQDQ ENLVLNEVYL GKEKFDSVHS KYMGRTSFDS DSWTLRLHNL QIKDKGLYQC IIHHKKPTGM IRIHQMNSEL SVLANFSQPE IVPISNITEN VYINLTCSSI HGYPEPKKMS VLLRTKNSTI EYDGIMQKSQ DNVTELYDVS ISLSVSFPDV TSNMTIFCIL ETDKTRLLSS PFSIELEDPQ PPPDHIPHHH HHH |
Storage & Handling
−| Storage | Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles |
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| Form/Appearance | Sterile Filtered colorless solution. |
| Buffer/Preservatives | CD86 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol. |
| Expiration Date | 6 months from date of receipt. |
| Disclaimer | For research use only |
Alternative Names
−Similar Products
−Human B7-2 Protein, mFc-His Tag [orb689395]
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 52.4 kDa after removal of the signal peptide.
Mammalian
10 μg, 50 μg, 100 μgRecombinant Cynomolgus B7-2 Protein [orb2994271]
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 52.5 KDa. Observed: 70-100 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgRecombinant Mouse B7-2 Protein [orb2994404]
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 52.2 KDa. Observed: 68-95 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgRecombinant Human B7-2 Protein [orb2995097]
Unconjugated
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 26.69 KDa. Observed: 57-66 KDa, reducing conditions
10 μg, 50 μg, 500 μg, 1 mgRecombinant Human B7-2 Protein (Biotin) [orb2993754]
Biotin
SDS-PAGE: Greater than 95% as determined by reducing SDS-PAGE.
Predicted: 28.4 KDa. Observed: 55-80 KDa, reducing conditions
20 μg, 100 μg

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