Rabbit Polyclonal SMURF2 Antibody

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     Anti-SMURF2 Antibody (C-term) at 1:2000 dilution + C2C12 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 86 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Western blot analysis of anti-SMURF2 Pab (Cat. #P33924) in 293 cell line lysate (35ug/lane). SMURF2(arrow) was detected using the purified Pab    

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     Hippocampal neurons were fixed at stage 3, stained with anti-Smurf2 (red) and anti-Kinesin-2 (green) antibodies, and analyzed by confocal microscopy. The panels show single confocal planes. (J. Biol. Chem. 2007 Nov 30;282(48):35259-35268)    

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     Hippocampal neurons were transfected 2 h after plating with expression vectors for EGFP, EGFP-tagged Par3-4N/2, Par3-PDZ2, Par3-PDZ3, Smurf2-HECT (HECT), Smurf2-HECT-C716A (HECT CA), and shRNA directed against mPar3 (Par3 RNAi), or vectors for the anti-Par3 shRNA and human Myc-Par3 (RNAi + h Par3) (green). Transfected cells were analyzed at 3 d.i.v. by staining with an anti-Smurf2 antibody (red). Axons are marked by arrowheads. The marked growth cones are shown at a higher magnification. Scale bars, 40 and 10 ?.  (J. Biol. Chem. 2007 Nov 30;282(48):35259-35268)    

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     Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.    

The SMURF2 (SMAD-specific E3 ubiquitin protein ligase 2) antibody is a crucial tool for studying the role of SMURF2. a HECT-domain E3 ubiquitin ligase involved in regulating cellular processes such as protein degradation, signal transduction, and cell homeostasis. SMURF2 primarily targets substrates for proteasomal degradation via ubiquitination, modulating key pathways like TGF-β/BMP signaling, Wnt/β-catenin, and Hippo-YAP. It interacts with SMAD proteins, leading to their ubiquitination and subsequent degradation, thereby fine-tuning TGF-β signaling. Dysregulation of SMURF2 is linked to cancer, fibrosis, and developmental disorders, with roles in promoting tumor metastasis (via EMT) or acting as a tumor suppressor, depending on context.

The SMURF2 antibody enables detection and quantification of SMURF2 expression in tissues or cell lines using techniques like Western blotting, immunohistochemistry, or immunofluorescence. Researchers employ it to investigate SMURF2’s interaction networks, post-translational modifications, and subcellular localization. Its application extends to studying pathological conditions, such as identifying SMURF2 overexpression in certain cancers or its downregulation in aging-related diseases. Recent studies also explore SMURF2’s involvement in autophagy, DNA repair, and viral infection, highlighting its multifaceted biological significance. Reliable SMURF2 antibodies are essential for elucidating its dual roles in oncogenesis and tissue homeostasis, aiding therapeutic target discovery.