SRP2028

Sigma-Aldrich

TFIIA, reconstituted human

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

Sinónimos:
TF2A1, TFIIA, TF2A2, MGC129969
NACRES:
NA.26
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

66 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

150 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... GTF2A1(2957), GTF2A2(2958)

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.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point F

Not applicable

Flash Point C

Not applicable

Certificado de Análisis
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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