추천 제품
제품명
RNA Polymerase II, C-terminal domain, GST tagged human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
생물학적 소스
human
재조합
expressed in E. coli
분석
≥70% (SDS-PAGE)
양식
frozen liquid
분자량
~68.1 kDa
포장
pkg of 10 μg
저장 조건
avoid repeated freeze/thaw cycles
색상
clear colorless
NCBI 수납 번호
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−70°C
유전자 정보
human ... POLR2A(5430)
생화학적/생리학적 작용
The CTD works as a binding scaffold for nuclear factors through its phosphorylation. It is suggested to be also involved in chromatin structure modification, DNA damage/repair, protein degradation and synthesis, RNA degradation, snRNA (small nuclear RNA) modification, and snoRNP (small nucleolar ribonucleoprotein) biogenesis.
The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA pol II in vivo: IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongation complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFb, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identified. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing.
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:
RNA polymerase II C-terminal domain required for enhancer-driven transcription.
Gerber HP, et al.
Nature, 374, 660-662 (1995)
Phosphorylation and functions of the RNA polymerase II CTD.
Phatnani HP and Greenleaf AL
Genes & Development, 20, 2922-2936 (2006)
T O'Brien et al.
Nature, 370(6484), 75-77 (1994-07-07)
The carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II is essential in vivo, and is found in either an unphosphorylated (IIa) or hyperphosphorylated (IIo) form. The Drosophila uninduced hsp70 and hsp26 genes, and the constitutively expressed beta-1
H Lu et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(22), 10004-10008 (1991-11-15)
The two forms of RNA polymerase II that exist in vivo, phosphorylated (IIO) and nonphosphorylated (IIA), were purified to apparent homogeneity from HeLa cells. The nonphosphorylated form preferentially binds to the preinitiation complex. RNA polymerase II in the complex was
The role of multisite phosphorylation in the regulation of RNA polymerase II activity.
M E Dahmus
Progress in nucleic acid research and molecular biology, 48, 143-179 (1994-01-01)
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