PD-L1 Antibody (MIH5) - BSA Free

Programmed-death ligand 1 (PD-L1), also known as CD274 and B7-H1, is a 33 kDa type I glycoprotein containing 290 amino acids (aa) belonging to the protein B7 family and serves as part of an immune checkpoint (1,2). PD-L1 contains an Ig-V and Ig-C-like extracellular domain, a transmembrane domain, and a cytoplasmic tail lacking canonical signaling motifs (2,3). PD-L1 is the ligand that binds the receptor programmed-death 1 (PD-1) which is highly expressed on active T cells (1-3). PD-L1 is typically upregulated by tumor cells and antigen presenting cells (APCs), but also expressed on T cells, B cells, macrophages, dendritic cells (DC), mast cells, and some non-immune cell types (1-3). In addition to the membrane-bound, PD-L1 is released from cells both in soluble form and bound to extracellular vesicles (4).

PD-L1 binding with receptor PD-1 results in phosphorylation of in the inhibitory tyrosine-based switch motif (ITSM) domain of PD-1, which leads to recruitment of Src homology 2 domain-containing protein tyrosine-phosphatase 2 (SHP-2) and eventual downstream phosphorylation of spleen tyrosine kinase (Syk) and phospholipid inositol-3-kinase (PI3K) (1,3). Under normal conditions, the PD-L1/PD-1 signaling axis helps maintain immune tolerance and prevent destructive immune responses by inhibiting T cell activity such as proliferation, survival, cytokine production, and cytotoxic T lymphocyte (CTL) cytotoxicity (1-3). In the tumor microenvironment (TME), however, the PD-L1/PD-1 signaling axis is hijacked to promote tumor cell survival and limit anti-tumor immune response (1,3). More precisely, tumor cells can escape killing and immune surveillance due to T cell exhaustion and apoptosis (1-3).

Given the role the PD-L1/PD-1 signaling axis plays in tumor cells' ability to evade immune surveillance, it has become a target of several immunotherapeutic agents in recent years (3,5). Antibody immunotherapies that target these inhibitory checkpoint molecules has shown great promise for cancer treatment (3,5). PD-L1 and PD-1 blocking agents have been approved for treatment in a number of cancers including melanoma, non-small cell lung cancer (NSCLC), urothelial carcinoma, and Merkel-cell carcinoma (3,5). In many cancers the expression of PD-L1 in the TME has predictive value for response to blocking agents (3). Pembrolizumab, for example, is a PD-1 inhibitor that has been approved by the FDA as a second-line therapy for treatment of metastatic NSCLC in patients whose tumors express PD-L1 with a Tumor Proportion Score (TPS) greater than 1%, but also for first-line treatment in cases where patients' tumors expression PD-L1 with a TPS greater than 50%) (5). The most promising cancer immunotherapy treatments seem to point to combination therapy with both anti-cancer drugs (e.g. Gefitibin, Metformin, Etoposide) with PD-L1/PD-1 antibody blockade inhibitors (e.g. Atezolizumab, Nivolumab) (6).

References

1. Han, Y., Liu, D., & Li, L. (2020). PD-1/PD-L1 pathway: current researches in cancer. American journal of cancer research, 10(3), 727-742.

2. Jiang, Y., Chen, M., Nie, H., & Yuan, Y. (2019). PD-1 and PD-L1 in cancer immunotherapy: clinical implications and future considerations. Human vaccines & immunotherapeutics, 15(5), 1111-1122. https://doi.org/10.1080/21645515.2019.1571892

3. Sun, C., Mezzadra, R., & Schumacher, T. N. (2018). Regulation and Function of the PD-L1 Checkpoint. Immunity, 48(3), 434-452. https://doi.org/10.1016/j.immuni.2018.03.014

4. Cha, J. H., Chan, L. C., Li, C. W., Hsu, J. L., & Hung, M. C. (2019). Mechanisms Controlling PD-L1 Expression in Cancer. Molecular cell, 76(3), 359-370. https://doi.org/10.1016/j.molcel.2019.09.030

5. Tsoukalas, N., Kiakou, M., Tsapakidis, K., Tolia, M., Aravantinou-Fatorou, E., Baxevanos, P., Kyrgias, G., & Theocharis, S. (2019). PD-1 and PD-L1 as immunotherapy targets and biomarkers in non-small cell lung cancer. Journal of B.U.ON. : official journal of the Balkan Union of Oncology, 24(3), 883-888.

6. Gou, Q., Dong, C., Xu, H., Khan, B., Jin, J., Liu, Q., Shi, J., & Hou, Y. (2020). PD-L1 degradation pathway and immunotherapy for cancer. Cell death & disease, 11(11), 955. https://doi.org/10.1038/s41419-020-03140-2

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 3 applications: ICC/IF, IHC-Fr, In Vivo.

Showing Publications 1 - 10 of 11. Show All 11 Publications. Collapse Publications.

Publications using NBP1-43262	Applications	Species
Kugeratski FG, LeBleu VS, Dowlatshahi DP et al. Engineered immunomodulatory extracellular vesicles derived from epithelial cells acquire capacity for positive and negative T cell co-stimulation in cancer and autoimmunity bioRxiv : the preprint server for biology 2023-11-04 [PMID: 37961535]
Wu Q, Wang W, Zhang C et al. Capturing nascent extracellular vesicles by metabolic glycan labeling-assisted microfluidics Nature communications 2023-10-17 [PMID: 37848408]
H. B. Deepak, Sabina Evan Prince, Pratima Deshpande Effect of baricitinib in regulating programmed death 1 and ligand programmed cell death ligand 1 through JAK/STAT pathway in psoriasis Indian Journal of Pharmacology 2022-01-01 [PMID: 35848689]
Roy S, Saha S, Gupta P et al. Crosstalk of PD-1 signaling with SIRT1/FOXO-1 axis in progression of visceral leishmaniasis J. Cell. Sci. 2019-03-25 [PMID: 30910830] (In Vivo, Mouse)	In Vivo	Mouse
Holokai L, Chakrabarti J, Broda T et al. Increased Programmed Death-Ligand 1 is an Early Epithelial Cell Response to Helicobacter pylori Infection PLoS Pathog. 2019-01-01 [PMID: 30703170] (ICC/IF, Human)	ICC/IF	Human
Chakrabarti J, Holokai L, Syu L et al. Hedgehog signaling induces PD-L1 expression and tumor cell proliferation in gastric cancer. Oncotarget 2018-12-21 [PMID: 30647844]
Samanta D, Park Y, Ni X et al. Chemotherapy induces enrichment of CD47+/CD73+/PDL1+ immune evasive triple-negative breast cancer cells Proc. Natl. Acad. Sci. U.S.A. 2018-01-24 [PMID: 29367423] (Mouse, Human) Details: This citation used the Alexa Fluor 488 form of this antbody		Mouse, Human
Sheng H, Wang Y, Jin Y et al. A critical role of IFNgamma in priming MSC-mediated suppression of T cell proliferation through up-regulation of B7-H1 Cell Res 2008-08-01 [PMID: 18607390] Details: This citation used the Biotin version of this antibody.
Tsushima F, Iwai H, Otsuki N et al. Preferential contribution of B7-H1 to programmed death-1-mediated regulation of hapten-specific allergic inflammatory responses Eur J Immunol 2003-10-01 [PMID: 14515261] Details: This citation used the Biotin version of this antibody.
Harding J, Vintersten-Nagy K, Shutova M, Yang H Induction of long-term allogeneic cell acceptance and formation of immune privileged tissue in immunocompetent Hosts bioRxiv 2019-07-30 (IHC-Fr, ICC/IF, Mouse)	IHC-Fr, ICC/IF	Mouse
He X, Smith SE, Chen S et al. Tumor-initiating stem cell shapes its microenvironment into an immunosuppressive barrier and pro-tumorigenic niche Cell reports 2021-09-07 [PMID: 34496236]
Show All 11 Publications. Collapse Publications.

Images	Ratings	Applications	Species	Date	Details
	4 reviewed by: Verified Customer	ICC	Human	06/21/2017	View Summary Application Immunocytochemistry Sample Tested Blood mononuclear cells (PBMCs) Species Human

Array NBP1-43262

• PD-L1 Antibodies
• PD-L1 Antibody Pairs
• PD-L1 Lysate
• PD-L1 Proteins
• PD-L1 Proteins and Enzymes
• PD-L1 ELISAs