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Key Documents

SRP2008

Sigma-Aldrich

TFIIF (RAP30 subunit) human

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

Sinónimos:

BTF4, RAP30, TF2F2, TFIiF

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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

~28.4 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

600 μg/mL

technique(s)

western blot: suitable

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... GTF2F2(2963)

Biochem/physiol Actions

The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP30) subunits that form a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. The RAP30 subunit of TFIIF contains two distinct regions with sequence similarity to E. coli factors and can deliver RNA polymerase II to the promoter to support transcription initiation in the absence of RAP74.

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


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S McCracken et al.
Science (New York, N.Y.), 253(5022), 900-902 (1991-08-23)
RAP30/74 is a heteromeric general transcription initiation factor that binds to mammalian RNA polymerase II. The RAP30 subunit contains a region that is similar in amino acid sequence to the RNA polymerase-binding domain of the Escherichia coli transcription initiation factor
M Sopta et al.
The Journal of biological chemistry, 260(18), 10353-10360 (1985-08-25)
We have used affinity chromatography on columns containing immobilized calf thymus RNA polymerase II to isolate three phosphoproteins (RAP72, RAP38, and RAP30) that bind directly to RNA polymerase II. All could be isolated from cell nuclei, and all three could
M Sopta et al.
Nature, 341(6241), 410-414 (1989-10-05)
RAP30/74 is a heteromeric general transcription initiation factor which binds to RNA polymerase II. Here we report that preparations of RAP30/74 contain an ATP-dependent DNA helicase whose probable function is to melt the DNA at transcriptional start sites. The sequence

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