重组D. melanogaster GAGA蛋白(ab51306)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
描述
-
产品名称
重组D. melanogaster GAGA蛋白 -
纯度
> 95 % SDS-PAGE.
GAGA-POZ domain was overexpressed in E.coli and purified by using conventional chromatography techniques. -
表达系统
Escherichia coli -
Accession
-
蛋白长度
Protein fragment -
无动物成分
No -
性质
Recombinant -
-
种属
Drosophila melanogaster -
序列
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ TVTKDDYTTH -
氨基酸
1 to 130
-
-
描述
重组D. melanogaster GAGA蛋白
技术指标
Our Abpromise guarantee covers the use of ab51306 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
-
应用
SDS-PAGE
-
形式
Liquid -
Concentration information loading...
制备和贮存
-
稳定性和存储
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
pH: 7.40
Constituents: 0.238% HEPES, 0.145% Sodium chloride
常规信息
-
别名
- GAF
- GAGA factor
- Nc70F
see all -
相关性
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. -
细胞定位
Nuclear
图片
-
SDS-PAGE - Recombinant Human GAGA protein (ab51306)ab51306 in 14% SDS-PAGE
实验方案
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
数据表及文件
-
Datasheet download
文献 (0)
ab51306 尚未被引用在任何文献中。
