Recombinant Human FCGR3B(NA1) protein, C-His-Avi Tag, Biotinylated
Product Description
Cat
IMP-648
Official Symbol
FCGR3B
Product Overview
Biotinylated Recombinant Human FCGR3B protein(Accession # O75015)(Gly 17-Ser 200), fused to C-His-Avi Tag, was expressed in HEK293.
Expression System
HEK293
Species
Human
Tag
C-His-Avi Tag, Biotinylated
Form
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Molecular Mass
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.
Protein length
Gly 17-Ser 200
Endotoxin
Less than 1.0 EU per μg by the LAL method.
Purity
>95% as determined by SDS-PAGE.
Storage
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:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Reconstitution
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.
SDS-PAGE
SDS-PAGE

Bioactivity-BLI 1

Loaded Biotinylated Human CD16b (NA1), His,Avitag (SPR & BLI verified) on SA Biosensor, can bind Rituximab with an affinity constant of 7.7 μM as determined in BLI assay.

Bioactivity-SPR 1
Bioactivity-SPR

Biotinylated Human CD16b (NA1), His,Avitag (SPR & BLI verified) 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.

Bioactivity-SPR 2
Bioactivity-SPR

Immobilized Biotinylated Human CD16b (NA1), His,Avitag (SPR & BLI verified) on SA Chip, can bind Herceptin with an affinity constant of 3.31 μM as determined in a SPR assay.

Data Sheet MSDS
Datasheet MSDS
For research or industrial raw materials, not for personal medical use!

Online Inquiry
Contact Info
Phone
  • 1-631-559-9269
    1-516-512-3133
Fax
  • 1-631-938-8127
Email
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