TNFRSF8/CD30 (E7E4D) XP® Rabbit mAb #25114
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90, 120 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| IHC Leica Bond | 1:50 |
| Immunohistochemistry (Paraffin) | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:400 |
| Flow Cytometry (Live) | 1:200 - 1:800 |
Storage
For a carrier free (BSA and azide free) version of this product see product #18445.
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the extracellular domain of human TNFRSF8/CD30 protein.
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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