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Key Documents

SRP2118

Sigma-Aldrich

RNA Polymerase II, RPB10 subunit, GST tagged human

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

Synonym(s):

RBP10, RPABC5, RPB10, RPB10beta, RPB7.6, hRPB7.6, hsRPB10b

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

Assay

≥85% (SDS-PAGE)

form

frozen liquid

mol wt

~33.6 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

300 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... POLR2L(5441)

Biochem/physiol Actions

The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. It is a zinc-binding protein with an atypical CX2CXnCC metal binding motif. RPB10 participates in protein-protein interactions with additional components of the polymerase holoenzyme. Experimentally, the binding of RPB10 to an RPB3-RPB11 (or RPAC40-RPAC19 in RNAPI/III) heterodimer is well characterized and persists in both eukaryal and archaeal RNAPs. Binding of RPB10 to this a2-like heterodimer through zinc-mediated hemi-coordination suggests an early role in holoenzyme assembly since the formation of the α2-complex is the first step in the assembly of the prokaryotic RNAPs.

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 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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C D Mackereth et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(12), 6316-6321 (2000-06-07)
The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a
N A Woychik et al.
Trends in biochemical sciences, 15(9), 347-351 (1990-09-01)
RNA polymerase II is the core of the complex apparatus that is responsible for the regulated synthesis of mRNA. A comprehensive knowledge of RNA polymerase II is essential to our understanding of the molecular mechanisms through which a variety of
N A Woychik et al.
Genes & development, 4(3), 313-323 (1990-03-01)
RNA polymerases I, II, and III share three subunits that are immunologically and biochemically indistinguishable. The Saccharomyces cerevisiae genes that encode these subunits (RPB5, RPB6, and RPB8) were isolated and sequenced, and their transcriptional start sites were deduced. RPB5 encodes

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