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Limited Edition Golden Llama is here! Check out how you can get one. 
Limited Edition Golden Llama is here! Check out how you can get one.
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This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™).
The protein has a calculated MW of 24.6 kDa. The protein migrates as 38-48 KDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
>95% as determined by SDS-PAGE.
>90% as determined by SEC-MALS.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
Biotinylated Human CD16b (NA1), His,Avitag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.
The purity of Biotinylated Human CD16b (NA1), His,Avitag (Cat. No. CDB-H82E4) is more than 90% and the molecular weight of this protein is around 37-55 kDa verified by SEC-MALS.
Biotinylated Human CD16b (NA1), His,Avitag (Cat. No. CDB-H82E4) captured on Biotin CAP- Series S Sensor Chip can bind Herceptin with an affinity constant of 8.32 μM as determined in a SPR assay (Biacore T200) (QC tested).
Immobilized Biotinylated Human CD16b (NA1), His,Avitag (Cat. No. CDB-H82E4) on SA Chip, can bind Herceptin with an affinity constant of 3.31 μM as determined in a SPR assay (Biacore T200) (Routinely tested).
Loaded Biotinylated Human CD16b (NA1), His,Avitag (Cat. No. CDB-H82E4) on SA Biosensor, can bind Rituximab with an affinity constant of 7.7 μM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.
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