TNFSF9

TNFSF9, a membrane-bound protein, comprises an extracellular glycosylated domain, a transmembrane domain, and an intracellular domain. The extracellular domain is a crucial part responsible for interacting with its receptor, 4-1BB (CD137). TNFSF9's primary function is to regulate the activity of immune cells, particularly T cells. When TNFSF9 binds to its receptor 4-1BB, it can activate T cells, enhancing their survival, proliferation, and effector functions.

Research on TNFSF9 has sparked widespread interest in the field of immunotherapy. Activation of the 4-1BB receptor can bolster the anti-tumor immune response of T cells. Therefore, researchers are developing TNFSF9-related therapeutic approaches, including 4-1BB agonists. The aim of these treatments is to enhance the immune system's ability to target cancer cells, improving the efficacy of immunotherapy. Additionally, the study of TNFSF9 contributes to a deeper understanding of immune regulation mechanisms, potentially offering new insights into the treatment of other immune-related and inflammatory diseases.

Popular Product

Recombinant Human Tumor necrosis factor ligand superfamily member 9(TNFSF9),partial (Active) CSB-MP023997HU1

Validated Data

SDS

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

ELISA

Activity: Measured by its binding ability in a functional ELISA. Immobilized TNFSF9 at 2 μg/ml can bind TNFRSF9（CSB-MP023984HU1）, the EC₅₀ is 2.671-3.702 ng/mL.