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Key Documents

COO/COA

SRP2008

TFIIF (RAP30 subunit) human

Name: TFIIF (RAP30 subunit) human
Brand: SIGMA

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

동의어(들):

BTF4, RAP30, TF2F2, TFIiF

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모든 사진(1)

About This Item

UNSPSC 코드:

12352202

NACRES:

NA.26

생물학적 소스

human

재조합

expressed in E. coli

분석

≥80% (SDS-PAGE)

형태

frozen liquid

분자량

~28.4 kDa

포장

pkg of 10 μg

저장 조건

avoid repeated freeze/thaw cycles

농도

600 μg/mL

기술

western blot: suitable

색상

clear colorless

NCBI 수납 번호

NM_004128

UniProt 수납 번호

P13984

배송 상태

dry ice

저장 온도

−70°C

유전자 정보

human ... GTF2F2(2963)

생화학적/생리학적 작용

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.

물리적 형태

Clear and colorless frozen liquid solution

제조 메모

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

시험 성적서(COA)

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문서 라이브러리 방문

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

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.