Recombinant Human STAT6 Protein (Baculovirus, His Tag) | PKSH030708

Recombinant Human STAT6 Protein (Baculovirus, His Tag) | PKSH030708 | Gentaur US, UK & Europe Disrtribition

Synonyms: Signal Transducer and Activator of Transcription 6; IL-4 Stat; STAT6;IL-4-STAT;STAT6B;STAT6C

Active Protein: N/A

Activity: 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.

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.

Fusion Tag: C-His

Species: Human

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 95.5 kDa

Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 20% gly, 0.3mM DTT

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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-?B 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-?B. 

Research Area: N/A