产品名称
TFIIA-p12 human, recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
biological source
human
recombinant
expressed in E. coli
assay
≥80% (SDS-PAGE)
form
frozen liquid
mol wt
~14.5 kDa
packaging
pkg of 10 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
300 μg/mL
color
clear colorless
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... GTF2A2(2958)
Biochem/physiol Actions
p12 is a small subunit ( γ ) of the transcription factor IIA and has been shown to be required for both basal and activated transcription. Recombinant p12, along with two other subunits ( α and β ) can potentiate transcriptional activation, whereas p12 along with β subunit is able to function in an anti-repression for reconstitued TFIIA, containing all three subunits.
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.
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
X Sun et al.
Genes & development, 8(19), 2336-2348 (1994-10-01)
Human TFIIA activity is composed of three subunits (alpha, beta, gamma). Here we report the isolation of a human cDNA clone encoding the gamma-subunit and the reconstitution of TFIIA activity from recombinant polypeptides (holo-TFIIA). Protein-protein interaction analysis established that the
J Ozer et al.
Genes & development, 8(19), 2324-2335 (1994-10-01)
TFIIA is thought to play an important role in transcriptional regulation in higher eukaryotes, but its precise function is unclear. A human cDNA encoding a protein with 45% identity to the small subunit of yeast TFIIA has been isolated. TFIIA
J DeJong et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(8), 3313-3317 (1995-04-11)
The human general transcription factor TFIIA is one of several factors involved in specific transcription by RNA polymerase II, possibly by regulating the activity of the TATA-binding subunit (TBP) of TFIID. TFIIA purified from HeLa extracts consists of 35-, 19-
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