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Merck

SRP2001

Sigma-Aldrich

TFIIA-p55 human

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

Synonym(e):

MGC129969, MGC129970, TF2A1, TFIIA

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About This Item

UNSPSC-Code:
12352202
NACRES:
NA.26

Biologische Quelle

human

Rekombinant

expressed in E. coli

Assay

≥80% (SDS-PAGE)

Form

frozen liquid

Mol-Gew.

~43.6 kDa

Verpackung

pkg of 10 μg

Lagerbedingungen

avoid repeated freeze/thaw cycles

Konzentration

500 μg/mL

Methode(n)

western blot: suitable

Farbe

clear colorless

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−70°C

Angaben zum Gen

human ... GTF2A1(2957)

Biochem./physiol. Wirkung

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 (a subunit), 19 kDa (b subunit) and 12 kDa (g subunit). The a and b 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 (g subunit), retains native TFIIA activity for reconstituted TFIIA, containing all three subunits.

Physikalische Form

Clear and colorless frozen liquid solution

Angaben zur Herstellung

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

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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
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 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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