Recombinant Human 4-1BB/TNFRSF9 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When recombinant human 4-1BB Fc Chimera is Immobilized at 10 ng/mL (100 µL/well), the concentration of recombinant human 4-1BB Ligand (Catalog # 2295-4L) that produces 50% optimal binding response is found to be approximately 0.5‑2.5 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human 4-1BB/TNFRSF9/CD137 protein
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
44.8 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
50-65 kDa, reducing conditions
Publications
Read Publications using 838-4B in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human 4-1BB/TNFRSF9 Fc Chimera Protein, CF
4-1BB ligand receptor
41BB
4-1BB
CD137 antigen
CD137
CD137MGC2172
CDw137
FLJ43501
ILA
ILAhomolog of mouse 4-1BB
induced by lymphocyte activation (ILA)
interleukin-activated receptor, homolog of mouse Ly63
receptor protein 4-1BB
T cell antigen ILA
T-cell antigen 4-1BB homolog
T-cell antigen ILA
TNFRSF9
tumor necrosis factor receptor superfamily member 9
tumor necrosis factor receptor superfamily, member 9
Background
4-1BB, also known as CD137 and TNFRSF9, is an approximately 30 kDa transmembrane glycoprotein in the TNF receptor superfamily. 4-1BB functions in the development and activation of multiple immune cells (1). Mature human 4-1BB consists of a 163 amino acid (aa) extracellular domain (ECD) with four TNFR cysteine‑rich repeats, a 27 aa transmembrane segment, and a 42 aa cytoplasmic domain (2, 3). Within the ECD, human 4-1BB shares 60% aa sequence identity with mouse and rat 4-1BB. 4-1BB is expressed as a disulfide-linked homodimer on various populations of activated T cell including CD4+, CD8+, memory CD8+, NKT, and regulatory T cells (4-7) as well as on myeloid and mast cell progenitors, dendritic cells, mast cells, and bacterially infected osteoblasts (8-11). It binds with high affinity to the transmembrane 4-1BB Ligand/TNFSF9 which is expressed on antigen presenting cells and myeloid progenitor cells (3, 8). This interaction co‑stimulates the proliferation, activation, and/or survival of the 4-1BB expressing cell (3-7). It can also enhance the activation-induced cell death of repetitively stimulated T cells (3). Mice lacking 4-1BB show augmented T cell activation, perhaps due to its absence on regulatory T cells (12). 4-1BB can associate with OX40 on activated T cells, forming a complex that responds to either ligand and inhibits Treg and CD8+ T cell proliferation (13). Reverse signaling through 4-1BB Ligand inhibits the development of dendritic cells, B cells, and osteoclasts (8, 11) but supports mature dendritic cell survival and co‑stimulates the proliferation and activation of mast cells (9, 10). 4‑1BB activation enhances CD8+ T cell and NK cell mediated anti-tumor immunity (14). It also contributes to the development of inflammation in high fat diet-induced metabolic syndrome (15). Soluble forms of 4-1BB and 4-1BB Ligand circulate at elevated levels in the serum of rheumatoid arthritis and hematologic cancer patients, respectively (16, 17).
Wang, C. et al. (2009) Immunol. Rev. 229:192.
Schwarz, H. et al. (1993) Gene 134:295.
Alderson, M.R. et al. (1994) Eur. J. Immunol. 24:2219.
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