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Mouse Smad2 Protein (His & GST Tag)

7120426M23Rik,Madh2,Madr2,mMad2,Smad-2

Catalog Number P50727-M20B
Organism Species Mouse
Host Baculovirus-Insect Cells
Synonyms 7120426M23Rik,Madh2,Madr2,mMad2,Smad-2
Molecular Weight The recombinant mouse SMAD2/GST chimera consists of 703 amino acids and has a calculated molecular mass of 80 kDa. The recombinant protein migrates as an approximately 90 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse SMAD2 (Q62432-Isoform Long) (Ser2-Ser467) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Transcription Factors and Regulators |Smad Transcription Factors
Formulation Lyophilized from sterile 20mM Tris, 500mM Nacl, pH 8.0, 10% glycerol, 3mM DTT
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background SMAD2 is a member of the SMAD family. Members of this family mediate signal transduction by the TGF-beta/activin/BMP-2/4 cytokine superfamily from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD2 mediates the signal of the TGF-beta, and therefore regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. SMAD2 is the downstream signal transducers of TGF-beta-1 in human dental pulp cells. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. Phosphorylated SMAD2 is able to form a complex with SMAD4 or SARA. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.
Reference
  • Feng. et al., 2002, Mol Cell. 9 (1): 133-43.
  • Zhu Y. et al., 1997, J Biol Chem. 272 (15): 10035-40.
  • Zi Z. et al., 2012, FEBS Lett. 586 (14): 1921-8.