GAGA-POZ Domain, Recombinant, Drosophila melanogaster

The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.\n\nDescription: \nRecombinant Drosophila melanogaster GAGA-POZ produced in E.Coli is a single,non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14kD.\n\nSequence: \nMSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH\n\nStability: \nStore at 4 degrees C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degrees C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

G1017-60B

Size

10ug

Form

Supplied as a liquid in 10mM HEPES, pH 7.4 and 25mM sodium chloride.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. Repression by TTK69 of GAGA-mediated activation occurs in the absence of TTK69 binding to DNA and solely requires the contribution of the POZ/BTB domain of TTK69.\n\nJ Biol Chem 2004 Mar 12;279(11):9725-32\n\n2. batman Interacts with polycomb and trithorax group genes and encodes a BTB/POZ protein that is included in a complex containing GAGA factor.\n\nMol Cell Biol 2003 Feb;23(4):1181-95\n\n3. The N-terminal POZ domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity.\n\nJ Biol Chem 1999 Jun 4;274(23):16461-9\n\n4. Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology.\n\nEMBO J 1999 Feb 1;18(3):698-708\n\n5. Comparison of the GAGA factor genes of Drosophila melanogaster and Drosophila virilis reveals high conservation of GAGA factor structure beyond the BTB/POZ and DNA-binding domains.\n\nDev Genes Evol 1998 Oct;208(8):447-56