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Key Documents

SRP2013

Sigma-Aldrich

RNA Polymerase II Peptide

≥85% (SDS-PAGE), recombinant, expressed in E. coli

Synonim(y):

POLRA, RPB1, RPO2, RPOL2, hRPB220

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About This Item

Kod UNSPSC:
12352202
NACRES:
NA.26

product name

RNA Polymerase II, C-terminal human, recombinant, expressed in E. coli, ≥85% (SDS-PAGE)

pochodzenie biologiczne

human

rekombinowane

expressed in E. coli

Próba

≥85% (SDS-PAGE)

Postać

frozen liquid

masa cząsteczkowa

~42.2 kDa

opakowanie

pkg of 10 μg

warunki przechowywania

avoid repeated freeze/thaw cycles

stężenie

400 μg/mL

kolor

clear colorless

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−70°C

informacje o genach

human ... POLR2A(5430)

Opis ogólny

RNA polymerase II (eukaryotic) contains around 10 subunits with a combined molecular weight of 500,000Da. The subunit structure of this enzyme is conserved amongst eukaryotes, and this subunits structure shares similarities with that of RNA pol I and III. 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.

Działania biochem./fizjol.

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, designated 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 elongating 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.

Postać fizyczna

Clear and colorless frozen liquid solution

Uwaga dotycząca przygotowania

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Evolution of the RNA polymerase II C-terminal domain.
Stiller JW and Hall BD
Proceedings of the National Academy of Sciences of the USA, 99(9), 6091-6096 (2002)
4 Carboxy-terminal Domain of the Largest Subunit of Eukaryotic RNA Polymerase II.
Corden JL and Ingles CJ
Cold Spring Harbor molecular case studies, 81-107 (1992)
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
RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function.
Prelich G
Eukaryotic Cell, 1(2), 153-162 (2002)

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