Recombinant Mouse CD30/TNFRSF8 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When rmCD30 Ligand (Catalog # 732-CL) is immobilized at 200 ng/well, the concentration of rmCD30 Fc Chimera that produces 50% of the optimal binding response is found to be approximately 0.5‑2.5 ng/mL |
Source |
Mouse myeloma cell line, NS0-derived mouse CD30/TNFRSF8 protein
Met |
Mouse CD30 (Phe19 - Thr281) Accession # Q60846 |
IEGRDMD |
Human IgG1 (Pro100 - Lys330) |
6-His tag |
N-terminus |
| |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Met |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Tnfrsf8 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
55 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 |
90-100 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 under reducing conditions and visualized by silver stain |
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 Mouse CD30/TNFRSF8 Fc Chimera Protein, CF
Background
CD30, also known as Ki-1 antigen and TNFRSF8, is a 120 kDa type I transmembrane glycoprotein belonging to the TNF receptor superfamily (1, 2). Mature mouse CD30 consists of a 264 amino acid (aa) extracellular domain (ECD) with three cysteine-rich repeats, a 27 aa transmembrane segment, and a 190 aa cytoplasmic domain (3). In contrast, human CD30 includes an additional 90 aa in the ECD and contains six cysteine-rich repeats. Within common regions of the ECD, mouse CD30 shares 53% and 80% aa sequence identity with human and rat CD30, respectively. CD30 is normally expressed on antigen-stimulated Th cells and B cells (4 - 6). However, it is upregulated in Hodgkin’s disease (on Reed-Sternberg cells), other lymphomas, chronic inflammation, and autoimmunity (7). CD30 binds to CD30 Ligand/TNFSF8 which is expressed on activated Th cells, monocytes, granulocytes and medullary thymic epithelial cells (1, 5). CD30 signaling costimulates antigen-induced Th0 and Th2 proliferation and cytokine secretion but favors a Th2-biased immune response (8). In the absence of antigenic stimulation, it can still induce T cell expression of IL-13 (9). CD30 contributes to thymic negative selection by inducing the apoptotic cell death of CD4+CD8+ T cells (10, 11). In B cells, CD30 ligation promotes cellular proliferation and antibody production in addition to the expression of CXCR4, CCL3, and CCL5 (5, 12). An 85 ‑ 90 kDa soluble form of CD30 is shed from the cell surface by TACE-mediated cleavage (13, 14). Soluble CD30 retains the ability to bind CD30 Ligand and functions as an inhibitor of normal CD30 signaling (15).
- Kennedy, M.K. et al. (2006) Immunology 118:143.
- Tarkowski, M. (2003) Curr. Opin. Hematol. 10:267.
- Bowen, M.A. et al. (1996) J. Immunol. 156:442.
- Hamann, D. et al. (1996) J. Immunol. 156:1387.
- Shanebeck, S.D. et al. (1995) Eur. J. Immunol. 25:2147.
- Gruss, H.-J. et al. (1994) Blood 83:2045.
- Oflzoglu E. et al. (2009) Adv. Exp. Med. Biol. 647:174.
- Del Prete, G. et al. (1995) J. Exp. Med. 182:1655.
- Harlin, H. et al. (2002) J. Immunol. 169:2451.
- Amakawa, R. et al. (1996) Cell 84:551.
- Chiarle, R. et al. (1999) J. Immunol. 163:194.
- Vinante, F. et al. (2002) Blood 99:52.
- Hansen, H.P. et al. (1995) Int. J. Cancer 63:750.
- Hansen, H.P. et al. (2000) J. Immunol. 165:6703.
- Hargreaves, P.G. and A. Al-Shamkhani (2002) Eur. J. Immunol. 32:163.
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