Key features and details
- Rabbit polyclonal to Smad3 (phospho S208)
- Suitable for: WB, IHC-P
- Reacts with: Human
- Isotype: IgG
Product nameAnti-Smad3 (phospho S208) antibody
See all Smad3 primary antibodies
DescriptionRabbit polyclonal to Smad3 (phospho S208)
Specificityab138659 detects endogenous levels of Smad3 only when phosphorylated at S208
Tested applicationsSuitable for: WB, IHC-Pmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthesized phospho-peptide derived from the internal region of Human Smad3 around the phosphorylation site of Serine 208
- Jurkat whole cell lysate (ab7899)
Storage instructionsShipped at 4°C. Store at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 49% PBS, 50% Glycerol, 0.88% Sodium chloride
PBS is without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab138659 was purified from Rabbit antiserum. The antibody against non phosphopeptide was removed by chromatography using non phosphopeptide corresponding to the phosphorylation.
Our Abpromise guarantee covers the use of ab138659 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/1000. Predicted molecular weight: 48 kDa.|
|IHC-P||1/50 - 1/100. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.|
FunctionReceptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Involvement in diseaseColorectal cancer
Loeys-Dietz syndrome 3
Sequence similaritiesBelongs to the dwarfin/SMAD family.
Contains 1 MH1 (MAD homology 1) domain.
Contains 1 MH2 (MAD homology 2) domain.
DomainThe MH1 domain is required for DNA binding. Also binds zinc ions which are necessary for the DNA binding.
The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import.
The linker region is required for the TGFbeta-mediated transcriptional activity and acts synergistically with the MH2 domain.
modificationsPhosphorylated on serine and threonine residues. Enhanced phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle dependent manner and inhibits both the transcriptional activity and antiproliferative functions of SMAD3. This phosphorylation is inhibited by flavopiridol. Maximum phosphorylation at the G(1)/S junction. Also phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1 and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is required for interaction with SMAD4, nuclear location and transactivational activity, and appears to be a prerequisite for the TGF-beta mediated phosphorylation in the linker region. Dephosphorylated in the C-terminal SXS motif by PPM1A. This dephosphorylation disrupts the interaction with SMAD4, promotes nuclear export and terminates TGF-beta-mediated signaling. Phosphorylation at Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Phosphorylated by PDPK1.
Acetylation in the nucleus by EP300 in the MH2 domain regulates positively its transcriptional activity and is enhanced by TGF-beta.
Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes.
Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation negatively regulates SMAD3 transcriptional responses during the course of TGF-beta signaling.
Cellular localizationCytoplasm. Nucleus. Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 (PubMed:15799969). Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (PubMed:16751101, PubMed:19289081). Co-localizes with LEMD3 at the nucleus inner membrane (PubMed:15601644). MAPK-mediated phosphorylation appears to have no effect on nuclear import (PubMed:19218245). PDPK1 prevents its nuclear translocation in response to TGF-beta (PubMed:17327236).
- Information by UniProt
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ab138659 has been referenced in 4 publications.
- Wang J et al. Microcystin-LR ameliorates pulmonary fibrosis via modulating CD206+ M2-like macrophage polarization. Cell Death Dis 11:136 (2020). PubMed: 32075954
- Feng F et al. The Protective Role of Tanshinone IIA in Silicosis Rat Model via TGF-ß1/Smad Signaling Suppression, NOX4 Inhibition and Nrf2/ARE Signaling Activation. Drug Des Devel Ther 13:4275-4290 (2019). PubMed: 31908414
- Xiao A et al. Statins affect human glioblastoma and other cancers through TGF-ß inhibition. Oncotarget 10:1716-1728 (2019). PubMed: 30899443
- Cui L et al. Jia-Shen decoction-medicated serum inhibits angiotensin-II induced cardiac fibroblast proliferation via the TGF-ß1/Smad signaling pathway. Mol Med Rep 14:1610-6 (2016). WB ; Rat . PubMed: 27315199