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Key Documents

SRP2007

Sigma-Aldrich

TFIIF (RAP74 subunit) human

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

同義詞:

BTF4, RAP74, TF2F1

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About This Item

分類程式碼代碼:
12352202
NACRES:
NA.26

生物源

human

重組細胞

expressed in E. coli

化驗

≥80% (SDS-PAGE)

形狀

frozen liquid

分子量

~59 kDa

包裝

pkg of 10 μg

儲存條件

avoid repeated freeze/thaw cycles

濃度

200 μg/mL

技術

western blot: suitable

顏色

clear colorless

NCBI登錄號

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−70°C

基因資訊

human ... GTF2F1(2962)

生化/生理作用

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.

外觀

Clear and colorless frozen liquid solution

準備報告

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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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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