STAT6 Protein (His Tag)

Signal transducer and activator of transcription 6, interleukin-4 induced Protein Datasheet

STAT6 Protein Product Information

• Synonym: D12S1644, IL-4-STAT, STAT6B, STAT6C
• Protein Construction: A DNA sequence encoding the human STAT6 isoform 1 (P42226-1) （Met 1-Trp 847）was fused with a polyhistidine tag at the C-terminus.
• Source: Human
• Expression Host: Baculovirus-Insect cells

STAT6 Protein QC Testing

• Purity: > 90 % as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ala 18
• Molecular Mass: The recombinant human STAT6 consists of 857 amino acids and predicts a molecular mass of 95.5 kDa. It migrates as an approximately 100 KDa band in SDS-PAGE in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from 0.2μm filtered solution of 20mM Tris, 500mM NaCl, pH 7.4, 20%gly, 0.3mM DTT
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: STAT6 protein

STAT6 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

STAT6 Protein Description

Signal transducer and activator of transcription 6 (STAT6) is a transcription factor that is activated by interleukin-4 (IL-4)-induced tyrosine phosphorylation and mediates most of the IL-4-induced gene expression. STAT6 plays a central role in exerting interleukin-4 (IL-4) mediated biological responses and is found to induce the expression of BCL2L1/BCL-XL, which is responsible for the anti-apoptotic activity of IL4. Transcriptional activation by STAT6 requires the interaction with coactivators like p300 and the CREB-binding protein (CBP). NF-κB and tyrosine-phosphorylated Stat6 can directly bind each other in vitro and in vivo, which suggest that the direct interaction between Stat6 and NF-κB may provide a basis for synergistic activation of transcription by IL-4 and activators of NF-κB.

References

1. Litterst CM. et al., 2001, J Biol Chem. 276 (49): 45713-21.
2. Stutz AM. et al., 1999, J Immunol. 163 (8): 4383-91.
3. Yang J. et al., 2002, EMBO J. 21 (18): 4950-8.