|Datasheet||Specific References||Reviews||Related Products||Protocols|
|ORF Clone of signal transducer and activator of transcription 6 DNA.|
|D12S1644, IL-4-STAT, STAT6B, STAT6C, STAT6|
|Identical with the Gene Bank Ref. ID sequence.|
|Whatman FTA elute card (Cat: WB120410) contains 5-10 μg of plasmid.|
|The Whatman FTA elute card can be stored at room temperature for three months under dry condition.|
The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Human STAT6 Gene cDNA Clone (full-length ORF Clone), expression ready, FLAG-tagged||HG13190-G-F|
|Human STAT6 Gene cDNA Clone (full-length ORF Clone), expression ready, His-tagged||HG13190-G-H|
|Human STAT6 Gene cDNA Clone (full-length ORF Clone), expression ready, Myc-tagged||HG13190-G-M|
|Human STAT6 Gene cDNA Clone (full-length ORF Clone), expression ready, untagged||HG13190-G-N|
|Human STAT6 Gene cDNA Clone (full-length ORF Clone), expression ready, HA-tagged||HG13190-G-Y|
|Product name||Product name|
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.