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Key Documents

SRP2115

Sigma-Aldrich

RNA Polymerase II, p33 subunit, GST tagged human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Synonym(s):

RPB3, RPB31, hRPB33, hsRPB3

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

~59.1 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

150 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... POLR2C(5432)

Biochem/physiol Actions

In human, RPB3 is encoded by the POLR2C gene. This gene encodes the third largest subunit of RNA polymerase II. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Pol II is the central component of the basal RNA polymerase II transcription machinery. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. In the pol II complex, RPB3 interacts with RPB5 and the RPB3-RPB5 interaction is intensified in the presence of three subunits, RPB7, RPB8 and RPB11. Besides, RPB3 also interacts with RPB. RPB3 is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor Myogenin. RPB3 also interact with IGFBP3.

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

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Corbi, N., et al.
Faseb Journal, 10, 10963-10963 (2002)
J Acker et al.
The Journal of biological chemistry, 272(27), 16815-16821 (1997-07-04)
As an initial approach to characterizing the molecular structure of the human RNA polymerase II (hRPB), we systematically investigated the protein-protein contacts that the subunits of this enzyme may establish with each other. To this end, we applied a glutathione

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