FITC Anti-Mouse CD274 (PD-L1) Antibody

Mouse splenocytes stained with either FITC anti-Mouse PD-L1 clone 10F.9G2 (blue histogram) or an isotype control (gray histogram).

Cat #	Size	Price	Quantity
201309	25 tests	$55
201310	100 tests	$130

Bulk/Custom

Product Details

Clone	10F.9G2
Application	Flow Cytometry
Reactivity	Mouse
Format	FITC
Target Name	CD274, PD-L1, B7-H1
Isotype	Rat IgG2b
Antibody Type	Monoclonal
Regulatory Status	RUO
Formulation	Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 0.2% (w/v) BSA
Protein Concentration	Supplied at a lot-specific concentration.
Storage and Handling	The antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light. Do not freeze.
Recommended Usage	For flow cytometric staining, it is recommended to use 5 µL of this reagent per 0.5-1.0 million cells in a 100 µL volume. Optimal reagent performance should be determined by titration for each specific application. FITC has an excitation max at 493 nm and an emission max at 525 nm.
Excitation Laser	Blue Laser (488 nm)
RRID	AB_3739041
See All Formats	Clone 10F.9G2

Background Information

Programmed death-ligand 1 (PD-L1), also known as CD274 or B7-H1, is a transmembrane protein that plays a pivotal role in immune regulation by modulating T cell activity. PD-L1 is expressed on a wide range of cells, including antigen-presenting cells, epithelial cells, and many tumor cells. Its primary function is to bind to its receptor, programmed cell death protein 1 (PD-1), located on activated T cells. This interaction delivers an inhibitory signal that reduces T cell proliferation, cytokine production, and cytotoxicity, thereby maintaining immune homeostasis and preventing autoimmunity. However, in pathological contexts such as cancer, PD-L1 expression allows tumor cells to evade immune attack, creating an immunosuppressive microenvironment.

Structurally, PD-L1 is a type I transmembrane glycoprotein belonging to the B7 family of immune checkpoint molecules. The extracellular domain comprises two immunoglobulin-like regions—an IgV-like domain responsible for PD-1 binding and an IgC-like domain that stabilizes the molecule. The protein also contains a single transmembrane helix and a short cytoplasmic tail that lacks classical signaling motifs but may interact with intracellular partners influencing its stability and localization. The PD-L1–PD-1 complex adopts a well-characterized interface where the IgV domains of both molecules interact in a way that blocks T cell receptor-mediated activation signaling.

The main ligands of PD-L1 are PD-1 and CD80 (B7-1). While PD-1 engagement results in T cell inhibition, interaction with CD80 may yield bidirectional signaling effects depending on the cellular context. PD-L1 can be induced by inflammatory cytokines such as interferon-gamma (IFN-γ), linking innate immune responses to immune checkpoint modulation.

PD-L1 plays a major role in numerous diseases. Overexpression of PD-L1 is a hallmark of many cancers, including lung, melanoma, renal, and breast cancers, where it contributes to immune escape. Therapeutically, blocking the PD-1/PD-L1 axis with immune checkpoint inhibitors has revolutionized cancer treatment. Drugs such as pembrolizumab, nivolumab, and atezolizumab disrupt this inhibitory pathway, restoring antitumor T cell function. Moreover, PD-L1 is being explored as both a predictive biomarker for immunotherapy response and a target for novel therapies, including bispecific antibodies and CAR-T cells aimed at enhancing immune-mediated tumor clearance.

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