SRP2115
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
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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
Faseb Journal, 10, 10963-10963 (2002)
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