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Key Documents

COO/COA

SRP2007

TFIIF (RAP74 subunit) human

Name: TFIIF (RAP74 subunit) human
Brand: SIGMA

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

Synonym(s):

BTF4, RAP74, TF2F1

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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 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

200 μg/mL

technique(s)

western blot: suitable

color

clear colorless

NCBI accession no.

NM_002096

UniProt accession no.

P35269

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... GTF2F1(2962)

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. In addition to its role in transcription initiation, TFIIF can increase the specificity and efficiency of RNA polymerase II transcription, and can especially increase the rate of transcription elongation.

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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Factors involved in specific transcription by mammalian RNA polymerase II. Factors IIE and IIF independently interact with RNA polymerase II.

O Flores et al.

The Journal of biological chemistry, 264(15), 8913-8921 (1989-05-25)

The purification and characterization of transcription factor IIF (TFIIF), a factor required for transcription by the RNA polymerase II machinery, is described. TFIIF was isolated from the previously described IIE protein fraction. TFIIF enters into the transcription cycle via a

Isolation of three proteins that bind to mammalian RNA polymerase II.

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

Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II.