SRP2008
TFIIF (RAP30 subunit) human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Synonym(s):
BTF4, RAP30, TF2F2, TFIiF
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About This Item
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 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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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
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
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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