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SRP2109

Sigma-Aldrich

TFIIA, p55 subunit, GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

Synonym(s):

MGC129969, MGC129970, TF2A1, TFIIA

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

Assay

≥70% (SDS-PAGE)

form

frozen liquid

mol wt

~68.2 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

200 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... GTF2A1(2957)

Biochem/physiol Actions

The transcription factor IIA (TFIIA) has been shown to bind to the TBP-DNA complex and to increase the affinity of TBP for the TATA element. Human TFIIA consists of three subunits of 35 kDa ( α subunit), 19 kDa ( β subunit) and 12 kDa ( γ subunit). The α and β subunits are derived from the product, p55, of a single gene by an unknown mechanism. However, recombinant p55, in combination with a 12 kDa subunit ( γ subunit), retains native TFIIA activity.

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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S Buratowski et al.
Cell, 56(4), 549-561 (1989-02-24)
A native gel electrophoresis DNA binding assay was used to resolve complexes formed on the adenovirus Major Late Promoter by general transcription factors and RNA polymerase II. Five sets of complexes containing distinct components were identified. These complexes were generated
J DeJong et al.
Genes & development, 7(11), 2220-2234 (1993-11-01)
TFIIA is a transcription factor that, by interacting with the TATA-binding subunit (TBP) of TFIID, modulates transcription initiation by RNA polymerase II in vitro. By use of a mobility shift assay, TFIIA was purified from HeLa cells as a complex
J A Ranish et al.
The Journal of biological chemistry, 266(29), 19320-19327 (1991-10-15)
The general transcription factor TFIIA was purified from yeast. A key step in the purification was affinity chromatography using a column containing the adenovirus major late promoter with bound recombinant TFIID to which TFIIA binds with high affinity. TFIIA activity

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