生物来源
human
重组
expressed in E. coli
方案
≥70% (SDS-PAGE)
表单
frozen liquid
分子量
~51.5 kDa
包装
pkg of 10 μg
储存条件
avoid repeated freeze/thaw cycles
浓度
200 μg/mL
技术
western blot: suitable
颜色
clear colorless
NCBI登记号
UniProt登记号
运输
dry ice
储存温度
−70°C
基因信息
human ... GTF2E1(2960)
生化/生理作用
The human Transcription Factor IIE (TFIIE) is composed of 56 kDa ( α) and 34 kDa ( β) subunits and is shown to be a heterotetramer. The 56-kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA polymerase II in solution and joins the pre-initiation complex probably concomitant with RNA polymerase II and TFIIF.
外形
Clear and colorless frozen liquid solution
制备说明
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
Y Ohkuma et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(23), 9163-9167 (1990-12-01)
Human transcription factor TFIIE, a ubiquitous factor required for transcription initiation by RNA polymerase II, was purified to homogeneity by a combination of conventional and HPLC steps. The purified TFIIE contained equimolar amounts of 57-kDa (TFIIE-alpha) and 34-kDa (TFIIE-beta) polypeptides
J Inostroza et al.
The Journal of biological chemistry, 266(14), 9304-9308 (1991-05-15)
Mammalian RNA polymerase II transcription factor IIE (TFIIE) was purified to apparent homogeneity. The activity copurified with polypeptides of 34 and 56 kDa. The 56-kDa subunit was sufficient for low levels of transcription activity in a transcription system reconstituted in
M G Peterson et al.
Nature, 354(6352), 369-373 (1991-12-05)
The general transcription factor IIE (TFIIE) is an essential component of the eukaryotic RNA polymerase II initiation complex. We have isolated human complementary DNA clones for both the subunits of TFIIE. Using purified recombinant proteins we find that both subunits
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