₩681,065
예상 입고일2025년 5월 09일세부사항
생물학적 소스
human
재조합
expressed in E. coli
분석
≥80% (SDS-PAGE)
양식
frozen liquid
분자량
~76.2 kDa
포장
pkg of 10 μg
저장 조건
avoid repeated freeze/thaw cycles
농도
450 μg/mL
색상
clear colorless
NCBI 수납 번호
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−70°C
유전자 정보
human ... GTF2E1(2960)
생화학적/생리학적 작용
The human Transcription Factor IIE (TFIIE) is composed of 56 kDa and 34 kDa 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 preinitiation complex probably concomitant with RNA polymerase II and TFIIF.
물리적 형태
Clear and colorless frozen liquid solution
제조 메모
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
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
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
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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