Recombinant human OX40L/TNFSF4 protein (Fc Chimera Active) (ab206011)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 90% SDS-PAGE
- Endotoxin level:
- Active: Yes
- Tags: Fc tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies, ELISA, Flow Cyt
Preparation and Storage
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Alternative names
- CD 134L
- CD 252
- CD134 ligand
see all -
Function
Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production. -
Involvement in disease
Genetic variations in TNFSF4 influence susceptibility to systemic lupus erythematosus (SLE) [MIM:152700]. SLE is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue. It affects principally the skin, joints, kidneys and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system. Note=The upstream region of TNFSF4 contains a single risk haplotype for SLE, which is correlated with increased expression of both cell-surface TNFSF4 and TNFSF4 transcripts. Increased levels of TNFSF4 are thought to augment T cell-APC interaction and the functional consequences of T cell activation, thereby destabilizing peripheral tolerance. -
Sequence similarities
Belongs to the tumor necrosis factor family. -
Cellular localization
Membrane. - Information by UniProt
Images
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ELISA - Recombinant human OX40L/TNFSF4 protein (Fc Chimera Active) (ab206011)
Immobilized Recombinant human CD134 / OX40L receptor protein (Active) (ab221231) at 0.5 μg/mL (100 μL/well) can bind Recombinant human OX40L/TNFSF4 protein (ab206011) with a linear range of 2-63 ng/mL.
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Functional Studies - Recombinant human OX40L/TNFSF4 protein (Fc Chimera Active) (ab206011)FACS assay shows that recombinant Human OX40L/TNFSF4, Fc Tag can bind to 293T cell overexpressing human OX40. The concentration of OX40L/TNFSF4 used is 0.01 µg/ml.
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SDS-PAGE - Recombinant human OX40L/TNFSF4 protein (Fc Chimera Active) (ab206011)SDS-PAGE analysis of reduced ab206011, staining overnight with Coomassie Blue. DTT-reduced Protein migrates as 53-55 kDa in SDS-PAGE due to glycosylation.
