Human STAT6 Recombinant Protein (His Tag)(Discontinued)
Fig 1: Human STAT6 Recombinant Protein (His Tag)
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| Amount : | 200 µg |
| Purification : | > 90 % as determined by SDS-PAGE |
| Content : | Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 20% gly, 0.3mM DTT Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. |
| Storage condition : | Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| AA sequence : | Met1-Trp847 |
| Alternative Name : | D12S1644 Protein, IL-4-STAT Protein, STAT6B Protein, STAT6C Protein, |
Source : Baculovirus-Insect Cells
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 p3 and the CREB-binding protein (CBP). NF-kB and tyrosine-phosphorylated Stat6 can directly bind each other in vitro and in vivo, which suggest that the direct interaction between Stat6 and NF-?B may provide a basis for synergistic activation of transcription by IL-4 and activators of NF-kB.
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 p3 and the CREB-binding protein (CBP). NF-kB and tyrosine-phosphorylated Stat6 can directly bind each other in vitro and in vivo, which suggest that the direct interaction between Stat6 and NF-?B may provide a basis for synergistic activation of transcription by IL-4 and activators of NF-kB.
Endotoxin :< 1.0 EU per µg of the protein as determined by the LAL method
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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