TNFRSF8/CD30 Antibody #40804
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90 (precursor), 120 (mature) |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
TNFRSF8/CD30 Antibody recognizes endogenous levels of total TNFRSF8/CD30 protein.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human TNFRSF8/CD30 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
TNFRSF8/CD30 is a type-I transmembrane glycoprotein that is a member of the TNFR superfamily. CD30 is synthesized as a precursor protein that undergoes extensive post-translational modification before becoming embedded in the plasma membrane as a 120-kDa transmembrane protein (1,2). The expression of CD30 is upregulated in activated T cells and may trigger costimulatory signaling pathways upon its engagement (3,4). While its expression is normally restricted to subsets of activated T cells and B cells, CD30 expression is robustly upregulated in hematologic malignancies, such as Hodgkin lymphoma (HL), anaplastic large cell lymphoma (ALCL), and adult T-cell leukemia, thus making it an attractive target for therapeutic intervention (5,6). Research studies have suggested that in certain disease contexts, CD30 recruits TRAF2 and TRAF5 adaptor proteins to drive NF-kappa B activation, aberrant cell growth, and cytokine production (7-9). CD30 signaling is also regulated by TACE-dependent proteolytic cleavage of its ectodomain, which results in reduced CD30L-dependent activation of CD30+ cells (10,11).
- Froese, P. et al. (1987) J Immunol 139, 2081-7.
- Nawrocki, J.F. et al. (1988) J Immunol 141, 672-80.
- Del Prete, G. et al. (1995) J Exp Med 182, 1655-61.
- Gilfillan, M.C. et al. (1998) J Immunol 160, 2180-7.
- Stein, H. et al. (1985) Blood 66, 848-58.
- Chiarle, R. et al. (1999) Clin Immunol 90, 157-64.
- Horie, R. et al. (2002) Am J Pathol 160, 1647-54.
- Horie, R. et al. (2002) Oncogene 21, 2493-503.
- Horie, R. et al. (2004) Cancer Cell 5, 353-64.
- Hansen, H.P. et al. (2000) J Immunol 165, 6703-9.
- Gruss, H.J. et al. (1997) Immunol Today 18, 156-63.
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