Recombinant Human CD30/TNFRSF8 His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When
Recombinant
Human CD30 Ligand/TNFSF8 (Catalog # 1028-CL)
is
immobilized at 0.25 μg/mL
(100 μL/well), the concentration of Biotinylated Recombinant Human CD30/TNFRSF8 His-tag Avi-tag
(Catalog # AVI10239)
that produces 50% of the optimal binding response is 2-10 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human CD30/TNFRSF8 protein Human CD30/TNFRSF8 (Phe19-Lys379) Accession # P28908.1 | HHHHHH | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Phe19 |
Structure / Form |
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 |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
41 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 |
82-98 kDa |
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 CD30/TNFRSF8 His-tag Avi-tag 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 human CD30 consists of a 361 amino acid (aa) extracellular domain (ECD) with six cysteine-rich repeats, a 28 aa transmembrane segment, and a 188 aa cytoplasmic domain (3). In contrast, mouse and rat CD30 lack 90 aa of the ECD and contain only three cysteine-rich repeats. Within common regions of the ECD, human CD30 shares 53% and 49% aa sequence identity with mouse and rat CD30, respectively. Alternate splicing of human CD30 generates an isoform that includes only the C‑terminal 132 aa of the cytoplasmic domain. CD30 is normally expressed on antigen-stimulated Th cells and B cells (4‑6). However, it is up‑regulated 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 co‑stimulates 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.
- Durkop, H. et al. (1992) Cell 68:421.
- 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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