Skip to Content
Merck
All Photos(1)

Key Documents

SRP2013

Sigma-Aldrich

RNA Polymerase II Peptide

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

Synonym(s):

POLRA, RPB1, RPO2, RPOL2, hRPB220

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

product name

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

biological source

human

recombinant

expressed in E. coli

Assay

≥85% (SDS-PAGE)

form

frozen liquid

mol wt

~42.2 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

400 μg/mL

color

clear colorless

NCBI accession no.

NM_000937

UniProt accession no.

P24928

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... POLR2A(5430)

Related Categories

General description

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.

Biochem/physiol Actions

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.

Physical form

Clear and colorless frozen liquid solution

Preparation Note

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function.
Prelich G
Eukaryotic Cell, 1(2), 153-162 (2002)
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)
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)
Zhiqiang Wu et al.
PloS one, 6(3), e18157-e18157 (2011-04-13)
Nuclear factor κB (NF-κB)-mediated pathways have been widely implicated in cell survival, development and tumor progression. Although the molecular events of determining NF-κB translocation from cytoplasm to nucleus have been extensively documented, the regulatory mechanisms of NF-κB activity inside the
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service