Anti-Phospho-SMAD3 (Ser423)(S12-365R)
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Description :Rabbit Polyclonal Antibody
Species :
Tag :
Expression System:
Sequence :
Specificity :Recognizes the human SMAD3 protein phosphorylated at Serine425 and Serine425
Cited Applications :ELISA, IHC, WB
Ideal working dilutions for each application should be empirically determined by the investigator
Cross Reactivity :Human, Xenopus laevis, Xenopus tropicalis, zebrafish, rat, mouse, swine, bovine and chicken.
Host Isotype / Clone# :Rabbit, IgG
Immunogen :The antibody was produced against synthesized synthesized peptide corresponding to amino acids 417-425 of human SMAD3 protein.
Purification :Immunoaffinity chromatography
Stability :1yr at –20oC from date of shipment
Sample Data :Anti-Phospho-SMAD3 (Ser423) was used at 2.5 µg/ml to detect signal in a variety of tissues including multi-human, multi-brain and multi-cancer slides. This image shows strong nuclear staining in the majority of epidermal keratinocytes at 40X. Tissue was formalin-fixed and paraffin embedded. The image shows localization of the antibody as the precipitated red signal, with a hematoxylin purple nuclear counterstain.
Sample Data :Western Blot of Rabbit anti-SMAD3 pS423 pS425 antibody- HEK293 lysate.
Scientific Background :SMAD3 is a direct mediator of transcriptional activation by the TGFβ receptor. The activity of SMAD3 is regulated by the TGFβ receptors, and SMAD3 is phosphorylated and associated with the ligand-bound receptor complex. TGFβ stimulation leads to phosphorylation and activation of SMAD3, which form a complex with SMAD4 that accumulate in the nucleus and regulate transcription of target genes such as CDK inhibitor (1). SMAD3 containing a C-terminal truncation acts as a dominant-negative inhibitor of the normal TGFβ response. SMAD3 is a major physiologic substrate of the G1 cyclin-dependent kinases CDK4 and CDK2 (2)
References :
1. Inman, G. J. et al: Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-beta receptor activity. Molec. Cell 10: 283-294, 2002.
2. Matsuura, I. et al: Cyclin-dependent kinases regulate the antiproliferative function of Smads. Nature 430: 226-231, 2004.
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Research Areas :AKT/PKB Pathway, Angiogenesis, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Inflammation, JAK/STAT Pathway, JNK/SAPK Pathway, NfkB Pathway, WNT Signaling