PathScan®Phospho-SMAD2 (Ser465/467)/SMAD3 (Ser423/425) Sandwich ELISA Kit#12001,Cell Signaling Technology (CST),12001

PathScan®Phospho-SMAD2 (Ser465/467)/SMAD3 (Ser423/425) Sandwich ELISA Kit recognizes endogenous levels of phospho-SMAD2 (Ser465/467) and SMAD3 (Ser423/425) proteins in human cells, as shown in Figure 1. This kit sensitivity is shown in Figure 2. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.

Reactivity

Human, Mouse, Mink

Platform ID

BAB709416312

Cell Signaling Technology (CST)

Headquarters

3 Trask Lane Danvers, MA 01923

Contact

Tel: 877-616-2355,978-867-2388
Fax: 877-616-2355

Product Specifications
Scientific Background
Synonyms

Specifications

NamePathScan®Phospho-SMAD2 (Ser465/467)/SMAD3 (Ser423/425) Sandwich ELISA Kit#12001
Cat. No.12001
Accession NumberP84022, Q15796
Gene ID (Entrez)84022, 15796, 4088, 4087
ReactivityHuman, Mouse, Mink
Regulatory StatusResearch Use Only

Scientific Background

Members of the SMAD family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of SMADs have been defined: the receptor-regulated SMADs (R-SMADs), which include SMAD1, 2, 3, 5, and 9; the common-mediator SMAD (co-SMAD), SMAD4; and the antagonistic or inhibitory SMADs (I-SMADs), SMAD6 and 7 (1-5). Activated type I receptors associate with specific R-SMADs and phosphorylate them on a conserved carboxy-terminal SSXS motif. The phosphorylated R-SMADs dissociate from the receptor and form a heteromeric complex with SMAD4, initiating translocation of the heteromeric SMAD complex to the nucleus. Once in the nucleus, SMADs recruit a variety of DNA binding proteins that function to regulate transcriptional activity (6-8).Heldin, C.H. et al. (1997)Nature390, 465-71.Attisano, L. and Wrana, J.L. (1998)Curr Opin Cell Biol10, 188-94.Derynck, R. et al. (1998)Cell95, 737-40.Massagué, J. (1998)Annu Rev Biochem67, 753-91.Whitman, M. (1998)Genes Dev12, 2445-62.Wrana, J.L. (2000)Sci STKE2000, re1.Attisano, L. and Wrana, J.L. (2002)Science296, 1646-7.Moustakas, A. et al. (2001)J Cell Sci114, 4359-69.Alternate NamesDKFZp586N0721; DKFZp686J10186; hMAD-2; hMAD-3; hSMAD2; hSMAD3; HSPC193; HsT17436; JV15-2; JV18; JV18-1; LDS1C; LDS3; MAD homolog 2; MAD homolog 3; mad homolog JV15-2; mad protein homolog; Mad protein homolog; Mad-related protein 2; MAD, mothers against decapentaplegic homolog 2; MAD, mothers against decapentaplegic homolog 3; Mad3; MADH2; MADH3; MADR2; MGC22139; MGC34440; MGC60396; mother against DPP homolog 2; Mothers against decapentaplegic homolog 2; Mothers against decapentaplegic homolog 3; Mothers against DPP homolog 2; Mothers against DPP homolog 3; Sma- and Mad-related protein 2; SMA- and MAD-related protein 3; SMAD 2; SMAD 3; SMAD family member 2; SMAD family member 3; SMAD, mothers against DPP homolog 2; SMAD, mothers against DPP homolog 3; SMAD2; SMAD3

Synonyms

DKFZp586N0721; DKFZp686J10186; hMAD-2; hMAD-3; hSMAD2; hSMAD3; HSPC193; HsT17436; JV15-2; JV18; JV18-1; LDS1C; LDS3; MAD homolog 2; MAD homolog 3; mad homolog JV15-2; mad protein homolog; Mad protein homolog; Mad-related protein 2; MAD, mothers against decapentaplegic homolog 2; MAD, mothers against decapentaplegic homolog 3; Mad3; MADH2; MADH3; MADR2; MGC22139; MGC34440; MGC60396; mother against DPP homolog 2; Mothers against decapentaplegic homolog 2; Mothers against decapentaplegic homolog 3; Mothers against DPP homolog 2; Mothers against DPP homolog 3; Sma- and Mad-related protein 2; SMA- and MAD-related protein 3; SMAD 2; SMAD 3; SMAD family member 2; SMAD family member 3; SMAD, mothers against DPP homolog 2; SMAD, mothers against DPP homolog 3; SMAD2; SMAD3

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