This protein carries a mouse IgG1 Fc tag at the C-terminus , and has a calculated MW of 51.6 kDa. The predicted N-terminus is Phe 19. The reducing (R) protein migrates as 65-85 kDa in SDS-PAGE due to glycosylation and the non-reducing (NR) protein migrates as 130-170 kDa.
>92% as determined by SDS-PAGE.
>90% as determined by SEC-HPLC.
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.
No activity loss is observed after storage at:
Human PD-L1, mouse IgG1 Fc Tag on SDS-PAGE under reducing (R) and no-reducing (NR) conditions. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 92%.
The purity of Human PD-L1 Protein, mouse IgG1 Fc Tag, low endotoxin (Cat.# PD1-H52A3) was more than 90% as determined by SEC-HPLC.
Immobilized Human PD-L1, mouse IgG1 Fc Tag (Cat. No. PD1-H52A3) at 5 μg/mL ( 100 μl/well ) can bind Biotinylated Human PD-1, His Tag & Fc tag (Cat. No. PD1-H82F2) with a linear range of 0.05-0.2 μg/mL (Routinely tested).
Flow Cytometry assay shows that recombinant Human PD-L1, mouse IgG1 Fc Tag (Cat.No. PD1-H52A3) can bind to 293 cell overexpressing human PD-1. The concentration of PD-L1 used is 0.1ug/ml (Routinely tested).
FACS analysis shows that the binding of Human PD-L1, mouse IgG1 Fc Tag to 293 overexpressing PD-1 was inhibited by increasing concentration of neutralizing anti-PD-1 antibody. The concentration of PD-L1 used is 1ug/ml. The IC50 is 0.145 μg/mL (Routinely tested).
Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.
Price(USD) : $280.00
Price(USD) : $1600.00
This web search service is supported by Google Inc.