Mouse Monoclonal SMAD1 Antibody

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     All lanes : Anti-SMAD1 Antibody at 1:2000 dilution Lane 1: HT-1080 whole cell lysate Lane 2: Hela whole cell lysate Lane 3: 293 whole cell lysate Lysates/proteins at 20 µg per lane.   Secondary Goat Anti-mouse IgG,    (H+L),   Peroxidase conjugated at 1/10000 dilution.   Predicted band size : 60 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Immunofluorescent analysis of 4% paraformaldehyde-fixed, 0.1% Triton X-100 permeabilized HeLa (human cervical epithelial adenocarcinoma cell line) cells labeling SMAD1 with P34374 at 1/25 dilution, followed by Dylight® 488-conjugated goat anti-mouse IgG secondary antibody at 1/200 dilution (green). Immunofluorescence image showing nucleus and weak cytoplasm staining on HeLa cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin at 1/100 dilution (red).  The nuclear counter stain is DAPI (blue).    

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     P34374 staining SMAD1 in human colon tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

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     P34374 staining SMAD1 in human skeletal muscle tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

SMAD1 is a critical intracellular signaling molecule belonging to the SMAD family, which mediates transforming growth factor-beta (TGF-β) superfamily signaling, particularly bone morphogenetic protein (BMP) pathways. As a receptor-regulated SMAD (R-SMAD), SMAD1 is activated through phosphorylation by BMP type I receptors upon ligand binding. This triggers its association with SMAD4 (Co-SMAD) and subsequent translocation to the nucleus, where the complex regulates transcription of target genes involved in embryonic development, cell differentiation, apoptosis, and tissue homeostasis.

SMAD1 antibodies are essential tools for studying BMP signaling dynamics. These antibodies specifically detect SMAD1 protein in various applications, including Western blotting, immunohistochemistry, immunofluorescence, and chromatin immunoprecipitation (ChIP). Researchers frequently use them to investigate SMAD1 activation status (phosphorylated vs. non-phosphorylated forms), subcellular localization, and protein-protein interactions. Commercially available antibodies are typically raised against epitopes in the N-terminal (MH1 domain) or C-terminal (MH2 domain) regions, with some targeting phosphorylation sites (e.g., Ser463/465).

Dysregulation of SMAD1 has been implicated in developmental disorders, cancer progression, and fibrotic diseases. SMAD1 antibodies thus play a vital role in both basic research and clinical studies, enabling the characterization of BMP pathway alterations in disease models and therapeutic interventions. Validation parameters for these antibodies often include knockout cell line verification and species cross-reactivity testing (human, mouse, rat). Careful antibody selection is crucial due to potential cross-reactivity with other SMAD family members (e.g., SMAD5. SMAD8/9) in some commercial products.