Anti-SMAD2 Antibody Picoband® (monoclonal, 3C4) Fluoro488 Conjugated

Smad2 (Mothers against decapentaplegic homolog 2), also known as MADR2, MADH2, SMAD family member 2 or SMAD2, is a protein that in humans is encoded by the SMAD2 gene. MAD homolog 2 belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. Eppert et al. mapped the MADR2 gene close to DPC4 at 18q21, a region which is frequently deleted in colorectal cancers. Riggins et al. mapped the human MADH2 gene to 18q21. Nakao et al. refined the localization of the SMAD2 gene to 18q21.1, approximately 3 Mb proximal to DPC4, by fluorescence in situ hybridization. SMAD2 mediates the signal of the transforming growth factor (TGF) -beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors.

Cadherins, Calcium Binding Proteins, Calcium Signaling, Cancer, Cell Adhesion, Cytoskeleton/ECM, Invasion/Microenvironment, Signal Transduction, Signaling Pathway

Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V (D) J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP.

1. Eppert, K., Scherer, S. W., Ozcelik, H., Pirone, R., Hoodless, P., Kim, H., Tsui, L.-C., Bapat, B., Gallinger, S., Andrulis, I. L., Thomsen, G. H., Wrana, J. L., Attisano, L.MADR2 maps to 18q21 and encodes a TGF-beta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma.Cell 86: 543-552, 1996. 2. Nakao, A., Roijer, E., Imamura, T., Souchelnytskyi, S., Stenman, G., Heldin, C.-H., ten Dijke, P.Identification of Smad2, a human Mad-related protein in the transforming growth factor-beta signaling pathway.J. Biol. Chem. 272: 2896-2900, 1997. 3. Riggins, G. J., Thiagalingam, S., Rozenblum, E., Weinstein, C. L., Kern, S. E., Hamilton, S. R., Willson, J. K. V., Markowitz, S. D., Kinzler, K. W., Vogelstein, B.Mad-related genes in the human.Nature Genet. 13: 347-349, 1996.

Nucleus. Endosome. Secreted. Cell membrane. Peripheral membrane protein. Extracellular side. Chromosome. Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment.