Recombinant Human CD40/TNFRSF5 Fc Avi-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human CD40 Ligand/TNFSF5 Fc (HEK293-expressed, (Catalog # 6420-CL)
mobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human CD40/TNFRSF5 Fc Chimera Avi-tag (Catalog # AVI10380) that produces 50% optimal binding is 0.0400-0.320 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human CD40/TNFRSF5 protein Human CD40/TNFRSF5 (Glu21-Arg193) Accession # P25942.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | |
|
Accession # |
|
N-terminal Sequence |
Glu21 |
Structure / Form |
Disulfide-linked homodimer, biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
48 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 |
61-66 kDa, under 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 with Trehalose. |
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 Human CD40/TNFRSF5 Fc Avi-tag Protein, CF
Background
CD40, also known as TNFRSF5, is a 45-50 kDa type I transmembrane glycoprotein member of the TNF receptor superfamily (1). Mature human CD40 consists of a 173 amino acid (aa) extracellular domain, a transmembrane domain, and a 62 aa cytoplasmic domain (2). The extracellular domain of human CD40 shares 58% and 56% aa sequence identity with mouse and rat CD40, respectively. An antagonistic soluble human CD40 splice variant contains an alternate sequence within the extracellular and transmembrane domains and lacks a cytoplasmic domain (3). CD40 is expressed on the surface of B cells, dendritic cells, macrophages, monocytes and platelets, as well as endothelial and epithelial cells (4, 5). Interaction of CD40 with its ligand, CD40 Ligand, leads to the aggregation of CD40 molecules resulting in the initiation of bidirectional intracellular signaling in both CD40 and CD40 Ligand expressing cells (6). CD40 ligation by CD40 Ligand promotes B cell activation and T cell-dependent humoral responses (7, 8). CD40 serves multiple functions in both hematopoietic and epithelial cancers and is a target for tumor immunotherapy (9, 10). Dysregulation of CD40/CD40 Ligand expression and interactions contributes to the immune deficiency associated with HIV infection and AIDS (11, 12). It is also implicated in the pathology of multiple cardiovascular diseases including atherosclerosis, atherothrombosis, and restenosis (13, 14).
- Banchereau, J. et al. (1994) Annu. Rev. Immunol. 12:881.
- Stamenkovic, I. et al. (1989) EMBO J. 8:1403.
- Eshel, D. et al. (2008) Mol. Immunol. 46:250.
- van Kooten, C. and J. Banchereau (1997) Curr. Opin. Immunol. 9:330.
- Schonbeck, U. et al. (1997) J. Biol. Chem. 272:19569.
- Eissner, G. et al. (2004) Cytokine Growth Factor Rev. 15:353.
- Rickert, R.C. et al. (2011) Immunol. Rev. 244:115.
- Elgueta, R. et al. (2009) Immunol. Rev. 229:152.
- Loskog, A.S. and A.G. Eliopoulos (2009) Semin. Immunol. 21:301.
- Hangalapura, B.N. et al. (2012) J. Gene Med. 14:416.
- Kornbluth, R.S. (2000) J. Leukoc. Biol. 68:373.
- Chougnet, C. (2003) J. Leukoc. Biol. 74:702.
- Pamukcu, B. et al. (2011) Ann. Med. 43:331.
- Hassan, G.S. et al. (2012) Immunobiology 217:521.
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