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Key Documents

R0884

Sigma-Aldrich

T7 RNA Polymerase

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

RNA Polymerase T7, RNA Polymerase, T7 from E. coli HMS 174/pAR1219

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

recombinant

expressed in E. coli

grade

for molecular biology

form

buffered aqueous solution

mol wt

98.8 kDa

concentration

10,000-50,000 U/mL

UniProt accession no.

foreign activity

DNase and RNase, none detected

storage temp.

−20°C

Gene Information

bacteriophage T7 ... T7p07(1261050)

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General description

T7 RNA polymerase is highly specific for the bacteriophage T7 promoter and terminator sequences. It is extensively used to prepare RNA transcripts for stuctural and metabolic studies. The RNA transcripts can be converted to probes for sensitive hybridization detection studies. T7 polymerase and dideoxynucleotides can be used to directly sequence DNA.

Components

T7 RNA Polymerase is supplied as a solution of 100 mM NaCl, 50 mM Tris-HCl (pH 7.9), 0.1 mM EDTA, 0.1% Triton X-100, 1 mM DTT, and 50% (v/v) glycerol.

Unit Definition

One unit will catalyze the incorporation of 1 nmol of rNTP into acid-precipitable material in 60 min at 37°C.

Analysis Note

Activity assay: 40 mM Tris-HCl, pH 7.9, 6 mM MgCl2, 4 mM spermidine, 10 mM DTT, 0.5 μM each rNTP + 10 μCi α-32P-UTP, 3-10 units of enzyme, and 1 μg of a 350 bp template are incubated for 10 min at 37°C in a total volume of 100 μl. Typical results are ≥50% incorporation of labeled nucleotide into ≥90% full-length transcript.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

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’.

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Characterization of T7-specific ribonucleic acid polymerase. 1. General properties of the enzymatic reaction and the template specificity of the enzyme.
M Chamberlin et al.
The Journal of biological chemistry, 248(6), 2235-2244 (1973-03-25)
Guillaume Allorent et al.
Plant molecular biology, 82(1-2), 59-70 (2013-03-16)
Arabidopsis seed formation is coupled with two plastid differentiation processes. Chloroplast formation starts during embryogenesis and ends with the maturation phase. It is followed by chloroplast dedifferentiation/degeneration that starts at the end of the maturation phase and leads to the
David L Shis et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(13), 5028-5033 (2013-03-13)
The construction of synthetic gene circuits relies on our ability to engineer regulatory architectures that are orthogonal to the host's native regulatory pathways. However, as synthetic gene circuits become larger and more complicated, we are limited by the small number
Sangjin Kim et al.
Science (New York, N.Y.), 339(6121), 816-819 (2013-02-16)
Allostery is well documented for proteins but less recognized for DNA-protein interactions. Here, we report that specific binding of a protein on DNA is substantially stabilized or destabilized by another protein bound nearby. The ternary complex's free energy oscillates as
Katsuhiko S Murakami
The Journal of biological chemistry, 288(13), 9126-9134 (2013-02-08)
Escherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual

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