Phospho-Smad3 (Ser423/425) Antibody (YA3477)
(Synonyms: SMAD3; MADH3; Mothers against decapentaplegic homolog 3; MAD homolog 3; Mad3; Mothers against DPP homolog 3; hMAD-3; JV15-2; SMAD family member 3; SMAD 3; Smad3; hSMAD3)Based on 1 publication(s) in Google Scholar
Phospho-Smad3 (Ser423/425) Antibody (YA3477) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Phospho-Smad3 (Ser423/425).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse
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Formulation:
Supplied in 10mM PBS, pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Publications Citing Use of MedChemExpress (MCE) Phospho-Smad3 (Ser423/425) Antibody (YA3477)
More
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:200 |
Product Details
Phospho-Smad3 (Ser423/425) Antibody (YA3477) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Phospho-Smad3 (Ser423/425).
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 55 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 48 kDa
A synthesized peptide derived from human Phospho-Smad3 (S423 + S425) RCS-pS-V-pS.
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 10mM PBS, pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Publications (1)
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Journal Impact Factor
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Most Recent
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Drug Resist Updat
Dynamic immunoediting by macrophages in homologous recombination deficiency-stratified pancreatic ductal adenocarcinoma. [Abstract]2024 Sep:76:101115. PMID: 39002266
Verification Images
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Immunohistochemical analysis of paraffin-embedded human gastric cancer tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam. -
Immunohistochemical analysis of paraffin-embedded human breast cancer tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam. -
Immunohistochemical analysis of paraffin-embedded human pancreatic cancer tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam. -
Immunohistochemical analysis of paraffin-embedded human hepatocellular carcinoma tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam. -
Immunohistochemical analysis of paraffin-embedded human liver cancer tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam. -
Immunohistochemical analysis of paraffin-embedded human hepatocellular carcinoma tissue using Phospho-Smad3 (Ser423/425) Antibody (YA3477). The section was pre-treated using heat mediated antigen retrieval with Tris/EDTA buffer (pH 9.0) for 20 minutes. The tissues were probed with the primary antibody (HY-P80854A, 1/100) overnight at 4℃. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with neutral balsam.
Background
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Function
SMAD3 is a receptor-regulated transcription factor in the TGF-β pathway, and activated TGF-β receptors phosphorylate SMAD3 to form SMAD complexes that regulate target-gene transcription[1]. Mechanistically, SMAD3 participates in cell proliferation, apoptosis, immune suppression, epithelial-mesenchymal transition, and extracellular matrix expression, making it useful for fibrosis, cancer progression, and inflammatory signaling studies[2][3]. In fibrosis models, SMAD3 acts as an important mediator of TGF-β profibrotic responses, and Smad3-deficient cells show reduced responses to selected chemotactic and matrix-related signals[3]. In cancer, SMAD3 can function as either a negative or positive regulator of carcinogenesis depending on cell type and tumor stage[2]. Compared with SMAD2, SMAD3 shows distinct regulation of TGF-β target genes and performs different functions in FOXH1-associated transcriptional control[4][5]. For experimental applications, SIS3 selectively inhibits TGF-β1-induced SMAD3 phosphorylation and SMAD3-SMAD4 interaction, making it a practical tool for testing SMAD3-dependent mechanisms[6].
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Subcellular Localization
Cytoplasm; Nucleus
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Isoforms & Post-Translational Modification
P84022 has 4 isomers: P84022-1: 48081 Da (predicted); P84022-2: 43237 Da (predicted); P84022-3: 35895 Da (predicted); P84022-4: 25722 Da (predicted).
Phosphorylated 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;Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation negatively regulates SMAD3 transcriptional responses during the course of TGF-beta signaling;Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding (PubMed:21947082). Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (PubMed:21947082). Ubiquitinated by RNF111, leading to its degradation: only SMAD3 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD3 and regulating its turnover (By similarity). Undergoes STUB1-mediated ubiquitination and degradation (PubMed:24613385) -
Subunit
Monomer; in the absence of TGF-beta (PubMed:9670020). Homooligomer; in the presence of TGF-beta (PubMed:9670020).
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SwissProt ID
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Synonyms
SMAD3; MADH3; Mothers against decapentaplegic homolog 3; MAD homolog 3; Mad3; Mothers against DPP homolog 3; hMAD-3; JV15-2; SMAD family member 3; SMAD 3; Smad3; hSMAD3
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Research Field
Signal Transduction
Documentation
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Data Sheet (262 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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User Guide for Antibodies (1077 KB)
References
[1]. Hata A, et al. TGF-β signaling from receptors to Smads. Cold Spring Harb Perspect Biol. 2016;8(9):a022061. [Content Brief]
[2]. Millet C, et al. Roles of Smad3 in TGF-beta signaling during carcinogenesis. Crit Rev Eukaryot Gene Expr. 2007;17(4):281-293. [Content Brief]
[3]. Flanders KC. Smad3 as a mediator of the fibrotic response. Int J Exp Pathol. 2004;85(2):47-64. [Content Brief]
[4]. Brown KA, et al. A tale of two proteins: differential roles and regulation of Smad2 and Smad3 in TGF-beta signaling. J Cell Biochem. 2007;101(1):9-33. [Content Brief]
[5]. Aragón E, et al. Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. Genes Dev. 2019;33(21-22):1506-1524. [Content Brief]
[6]. Jinnin M, et al. Characterization of SIS3, a novel specific inhibitor of Smad3, and its effect on transforming growth factor-beta1-induced extracellular matrix expression. Mol Pharmacol. 2006;69(2):597-607. [Content Brief]
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