TGF-β Antibody #3711
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 12, 25, 45 to 65 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
TGF-beta Antibody detects recombinant TGF-β1, TGF-β2, and TGF-β3. The antibody also detects endogenous levels of the TGF-β1 precursor proteins.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic peptide corresponding to a region in the carboxy terminus of TGF-beta1. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Transforming growth factor-β (TGF-β) proteins belong to the TGF-β superfamily of cytokines that play a critical role in regulating cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-3). TGF-β ligands elicit signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII) TGF-β receptors. Type I and type II receptors are serine/threonine kinases that form a heteromeric complex following ligand binding to the type II receptor. In response to ligand binding, the type II receptors form a stable complex with the type I receptors, triggering phosphorylation and activation of the type I receptor (4). The results in the recruitment of receptor-mediated SMADs (SMAD2, SMAD3), which are phosphorylated by the type I kinase in an SSXS domain in the C-terminus. This leads to recruitment of the co-SMAD (SMAD4), and subsequent translocation of this heteromeric SMAD complext to the nucleus, where it regulates transcription of target genes (5-7). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain. Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex (8).
There are three TGF-beta family members, designated TGF-β1, TGF-β2, and TGF-β3, which are encoded by distinct genes and are expressed in a tissue specific manner (10). TGF-β proteins are synthesized as precursor proteins that are cleaved and reassembled in association with other proteins to form latent complexes. Activation occurs by proteolytic release of TGF-β monomers, which dimerize to form the mature TGF-β ligands.
- Massagué, J. et al. (2000) Cell 103, 295-309.
- de Caestecker, M.P. et al. (2000) J Natl Cancer Inst 92, 1388-402.
- Derynck, R. et al. (2001) Nat Genet 29, 117-29.
- Derynck, R. and Feng, X.H. (1997) Biochim Biophys Acta 1333, F105-50.
- Miyazono, K. et al. (2000) Adv Immunol 75, 115-57.
- Massagué, J. (2000) Nat Rev Mol Cell Biol 1, 169-78.
- Derynck, R. et al. (1998) Cell 95, 737-40.
- López-Casillas, F. et al. (1991) Cell 67, 785-95.
- Kingsley, D.M. (1994) Genes Dev 8, 133-46.
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