SRP2007
TFIIF (RAP74 subunit) human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
别名:
BTF4, RAP74, TF2F1
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关于此项目
NACRES:
NA.26
UNSPSC Code:
12352202
Biological source:
human
Recombinant:
expressed in E. coli
Assay:
≥80% (SDS-PAGE)
Form:
frozen liquid
Mol wt:
~59 kDa
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.
UniProt accession no.
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.
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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
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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