Product Pathways - TGF-beta/Smad Signaling
TGF-β Receptor III Antibody #2519
|2519S||100 µl (10 western blots)||---||In Stock||---|
|2519||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Rat.
Specificity / Sensitivity
TGF-β Receptor III Antibody detects endogenous levels of the type III TGF-β receptor. This antibody does not cross-react with other family members at physiological conditions.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues in the extracellular domain of the type III TGF-β receptor. Antibodies are purified by protein A and peptide affinity chromatography.
Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). 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 (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).
The type III TGF-β receptor is upregulated during skeletal muscle differentiation (10).
- Massague, J. et al. (2000) Cell 103, 295-309.
- Caestecker, M.P. et al. (2000) J. Natl. Cancer Inst. 92, 1388-1402.
- Derynck, R. et al. (2001) Nature Genet. 29, 117-129.
- Miyazono, K. et al. (2000) Adv. Immunol. 75, 115-157.
- Derynck, R. et al. (1997) Biochim. Biophys. Acta. 1333, F105-150.
- López-Casillas, F. et al. (1991) Cell 67, 785-795.
- Wang, X.F. et al. (1991) Cell 67, 797-805.
- Derynck, R. et al. (1998) Cell 95, 737-740.
- Massague, J. et al. (2000) Nat. Rev. Mol. Cell Biol. 1, 169-178.
- Lopez-Casillas, F. et al. (2003) J. Biol. Chem. 278, 382-390.
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