Product nameAnti-Smad2 (phospho S467) antibody
See all Smad2 primary antibodies
DescriptionRabbit polyclonal to Smad2 (phospho S467)
Tested applicationsSuitable for: Dot blot, IHC-P, ICC/IFmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic peptide. This information is considered to be commercially sensitive.
- IHC-P: Human brain cortex. ICC/IF: HeLa cells.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.01% Sodium azide
Concentration information loading...
Our Abpromise guarantee covers the use of ab235265 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Dot blot||Use at an assay dependent concentration.|
|IHC-P||1/2000. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.|
|ICC/IF||Use a concentration of 15 µg/ml.|
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 SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma.
Tissue specificityExpressed at high levels in skeletal muscle, heart and placenta.
Sequence similaritiesBelongs to the dwarfin/SMAD family.
Contains 1 MH1 (MAD homology 1) domain.
Contains 1 MH2 (MAD homology 2) domain.
modificationsPhosphorylated on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases. Able to interact with SMURF2 when phosphorylated on Ser-465/467, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin.
In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation.
Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. Isoform short: Acetylation increases DNA binding activity in vitro and enhances its association with target promoters in vivo. Acetylation in the nucleus by EP300 is enhanced by TGF-beta.
Cellular localizationCytoplasm. Nucleus. Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1.
- Information by UniProt
- Drosophila, homolog of, MADR2 antibody
- hMAD-2 antibody
- HsMAD2 antibody
Immunohistochemistry analysis of Formalin/PFA-fixed paraffin-embedded human brain cortex tissue stained for Smad2 (phospho S467) using ab235265 at a 1/1000 dilution for 30 mins at RT, followed by a ready to use anti-rabbit poly HRP IgG for 8 mins at RT. Counterstained with hematoxylin.
HIER using citrate buffer for 20 mins was performed.
Dot Blot - Anti-Smad2 (phospho S467) antibody (ab235265 at 1 µg/ml).
Lanes 1-5: 100, 33.33, 11.11, 3.70, 1.23 ng.
Row A: Smad2 phospho-S467 - BSA Peptide.
Row B: Smad2 S467 - BSA Peptide.
Row C: AKT1 pS473 - BSA Peptide.
Row D: AKT1 S473 - BSA Peptide.
Row E: Scramble Sprouty - BSA Peptide.
Row F: BSA.
Exposure time of 10 secs.
Immunocytochemistry/ Immunofluorescence analysis of 4% PFA-fixed, 0.3% Triton X-100 permeabilized HeLa (Human epithelial cell line from cervix adenocarcinoma) cells stained for Smad2 (phospho S467) using ab235265 at 15 µg/ml overnight at 4°C. A donkey anti-rabbit IgG DyLight™ 488 was used as the secondary, 5 µg/ml for 1 hour at RT.
ab235265 has not yet been referenced specifically in any publications.