Recombinant Cynomolgus 4-1BB/TNFRSF9 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey 4-1BB/TNFRSF9/CD137 Fc Chimera is immobilized at 0.05 µg/mL (100 µL/well),
Recombinant
Human 4-1BB Ligand/TNFSF9 (Catalog # 2295-4L)
binds with an ED 50 of 0.25-1.25 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey 4-1BB/TNFRSF9/CD137 protein Cynomolgus Monkey 4-1BB/TNFRSF9 (Leu24-Gln186) Accession # XP_005544945 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Leu24 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
44 kDa. 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 |
56-66 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
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 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus 4-1BB/TNFRSF9 Fc Chimera Protein, CF
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, cynomolgus 4-1BB shares 95%, 57%, and 57% aa sequence identity
with human, mouse, and rat 4-1BB, respectively.
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.
- Wen, T. et al. (2002) J. Immunol. 168:4897.
- Pulle, G. et al. (2006) J. Immunol. 176:2739.
- Zheng, G. et al. (2004) J. Immunol. 173:2428.
- Kim, D. et al. (2008) J. Immunol. 180:2062.
- Lee, S. et al. (2008) Nat. Immunol.9:917.
- Choi, B.K. et al. (2009) J. Immunol. 182:4107.
- Nishimoto, H. et al. (2005) Blood 106:4241.
- Saito, K. et al. (2004) J. Biol. Chem. 279:13555.
- Lee, S. et al. (2005) J. Immunol. 174:6803.
- Ma, B.Y. et al. (2005) Blood 106:2002.
- Choi, B.K. et al. (2010) J. Immunol. 185:1404.
- Kim, C. et al. (2011) Diabetes 60:3159.
- Michel, J. et al. (1998) Eur. J. Immunol. 28:290.
- Salih, H.R. et al. (2001) J. Immunol. 167:4059.
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