生物源
human
重組細胞
expressed in E. coli
化驗
≥70% (SDS-PAGE)
形狀
frozen liquid
分子量
~35 kDa
包裝
pkg of 10 μg
儲存條件
avoid repeated freeze/thaw cycles
濃度
250 μg/mL
技術
western blot: suitable
顏色
clear colorless
NCBI登錄號
UniProt登錄號
運輸包裝
dry ice
儲存溫度
−70°C
基因資訊
human ... GTF2E2(2961)
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.
外觀
Clear and colorless frozen liquid solution
準備報告
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 2
閃點（°F）
Not applicable
閃點（°C）
Not applicable
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號，寫有 ‘Lot’或‘Batch’.。
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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