Pd l1 fc

Manufactured by Thermo Fisher Scientific

PD-L1-Fc is a recombinant fusion protein consisting of the extracellular domain of human Programmed Death-Ligand 1 (PD-L1) and the Fc region of human IgG1. It is a research-use-only product designed for use in immunological assays and other research applications.

Automatically generated - may contain errors

Lab products found in correlation

Multiskan fc photometer, by Thermo Fisher Scientific (1 mentions) Egfr fc, by R&D Systems (1 mentions) Streptavidin pe, by Thermo Fisher Scientific (1 mentions) Anti human igg fc biotin, by BioLegend (1 mentions) Fcr blocking reagent, by Miltenyi Biotec (1 mentions) Lsr 2 flow cytometer, by BD (1 mentions)

3 protocols using pd l1 fc

Quantifying Protein-Protein Interactions

Check if the same lab product or an alternative is used in the 5 most similar protocols

The human EGFR-Fc (EGFR-Fc, R&D Systems, cat# 344-ER) or human PD-L1-Fc (PD-L1-Fc, Peprotech, cat# 310–35) chimeras were immobilized (2.5 µg/ml in PBS) on Maxisorp 96-well plates (NUNC Brand Products, cat# 44240) overnight at 4°C. After washing and blocking, conditioned media or purified protein solution (1 µg/ml) was added and incubated for 1 hour at room temperature. The wells were washed and HRP-conjugated anti-poly Histidine (Sigma-Aldrich, cat# A7058), HRP-conjugated anti-FLAG (M2 clone, Sigma-Aldrich, cat# A8592), mouse anti-Myc (clone 9E10, Millipore, cat# 05–419) or HRP-conjugated goat anti-human IgG (GAH) (Sigma-Aldrich, cat# A0170) were added (1 µg/ml). After washing, in the case of mouse anti-Myc, GAM-HRP (1:2,000 dilution) (Jackson ImmunoResearch, cat# 115-085-166) was added for 1 hour at room temperature. Finally, after washing, the plate was developed using 100 μl 3,3′,5,5′-tetramethylbenzidine (TMB) (Sigma-Aldrich, cat# T0440) and stopped by 100 μl of 1 N H₂SO₄. Absorbance was read at 450–620 nm using Multiskan FC photometer (Thermo Scientific).

Rubio-Pérez L., Lázaro-Gorines R., Harwood S.L., Compte M., Navarro R., Tapia-Galisteo A., Bonet J., Blanco B., Lykkemark S., Ramírez-Fernández Á., Ferreras-Gutiérrez M., Domínguez-Alonso C., Díez-Alonso L., Segura-Tudela A., Hangiu O., Erce-Llamazares A., Blanco F.J., Santos C., Rodríguez-Peralto J.L., Sanz L, & Álvarez-Vallina L. (2023). A PD-L1/EGFR bispecific antibody combines immune checkpoint blockade and direct anti-cancer action for an enhanced anti-tumor response. Oncoimmunology, 12(1), 2205336.

+ Open protocol

+ Expand

Characterizing PD-L1 and PD-L2 Binding in HEK293T Cells

Check if the same lab product or an alternative is used in the 5 most similar protocols

Transiently transfected HEK293T cells were removed from the well, washed once, and stained with Live/Dead Aqua, as described above. Cells were washed once with complete culture medium and incubated (2.5 μg/100 μL/test, one hour at 37°C) with recombinant PD-L1-Fc (PeproTech, Cat: 310–35) or PD-L2-Fc (PeproTech, Cat: 310–38). The supernatant was removed, and cells were stained with anti-human IgG Fc-biotin (BioLegend, Clone: M1310G05, Cat: 410718, 1:50, one hour at 4°C in the dark) in FACS buffer supplemented with FcR Blocking Reagent (Miltenyi Biotec, 1:50) and 0.1% sodium azide. As a negative control, anti-human IgM-biotin (BioLegend, Clone: MHM-88, Cat: 314504, 1:50) and biotin-conjugated rat IgG2a isotype control (BioLegend, Clone: RTK2758, Cat: 400504, 1:50) antibodies were also used. Cells were washed once with FACS buffer and stained with streptavidin-PE (eBioscience, Cat: 12–4317-87, 1:100, one hour at 4°C in the dark) in FACS buffer supplemented with 0.1% sodium azide. Cells were washed twice with FACS buffer and acquired with a BD LSR II Flow Cytometer (BD Biosciences).

Ogishi M., Yang R., Aytekin C., Langlais D., Bourgey M., Khan T., Ali F.A., Rahman M., Delmonte O.M., Chrabieh M., Zhang P., Gruber C., Pelham S.J., Spaan A.N., Rosain J., Lei W.T., Drutman S., Hellmann M.D., Callahan M.K., Adamow M., Wong P., Wolchok J.D., Rao G., Ma C.S., Nakajima Y., Yaguchi T., Chamoto K., Williams S.C., Emile J.F., Rozenberg F., Glickman M.S., Rapaport F., Kerner G., Allington G., Tezcan I., Cagdas D., Hosnut F.O., Dogu F., Ikinciogullari A., Rao V.K., Kainulainen L., Béziat V., Bustamante J., Vilarinho S., Lifton R.P., Boisson B., Abel L., Bogunovic D., Marr N., Notarangelo L.D., Tangye S.G., Honjo T., Gros P., Boisson-Dupuis S, & Casanova J.L. (2021). Inherited PD-1 deficiency underlies tuberculosis and autoimmunity in a child. Nature medicine, 27(9), 1646-1654.

+ Open protocol

+ Expand

Chicken Immunization and Library Generation

Check if the same lab product or an alternative is used in the 5 most similar protocols

Chicken immunization and library generation were performed as previously described (56 (link)). In brief, two chickens (Gallus gallus domesticus) were immunized with CD16a or PD-L1, respectively. Five immunizations were performed for the CD16a-immunized animal on days 1, 14, 28, 42, and 56. For the first two immunizations, CD16a-Fc (produced in-house) was utilized, all subsequent immunizations were performed with a mixture of CD16a-Fc and TwinStrep-tagged CD16a (produced in-house). After the fourth immunization, the serum titer against both antigens was determined. The animal was sacrificed on day 63, followed by isolation of the spleen and RNA extraction. For the second chicken, an identical immunization plan was applied, utilizing PD-L1-Fc (PeproTech) as the antigen. All chicken immunizations, as well as sacrifice of the animal and subsequent RNA extraction from resurrected spleen cells, were performed at Davids Biotech GmbH. Experimental procedures and animal care were in accordance with EU animal welfare protection laws and regulations.

Bogen J.P., Carrara S.C., Fiebig D., Grzeschik J., Hock B, & Kolmar H. (2021). Design of a Trispecific Checkpoint Inhibitor and Natural Killer Cell Engager Based on a 2 + 1 Common Light Chain Antibody Architecture. Frontiers in Immunology, 12, 669496.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!