SRP2025
p52 human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
Sinónimos:
DFS70, LEDGF, MGC74712, PAIP, p52
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.26
Productos recomendados
biological source
human
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
frozen liquid
mol wt
~39 kDa
packaging
pkg of 10 μg
concentration
600 μg/mL
color
clear colorless
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PSIP1(11168)
Biochem/physiol Actions
The human p52 protein is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA polymerase II. The function of p52 is through interactions with transcriptional activators and the basal transcription machinery. In addition, p52 may also interact with several cellular proteins including the transcription coactivator PC4, the essential splicing factor ASF/SF2 and the nuclear protein nucleolin.
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
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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H Ge
Nucleic acids research, 28(2), e3-e3 (1999-12-22)
Protein-protein interactions have been widely used to study gene expression pathways and may be considered as a new approach to drug discovery. Here I report the development of a universal protein array (UPA) system that provides a sensitive, quantitative, multi-purpose
H Ge et al.
Molecular cell, 2(6), 751-759 (1999-01-14)
Increasing evidence suggests that pre-mRNA splicing can take place cotranscriptionally in vivo. However, insight into how these two processes are linked has been lacking. Here, we describe that a novel transcriptional coactivator, p52, interacts not only with transcriptional activators and
H Ge et al.
The EMBO journal, 17(22), 6723-6729 (1998-11-21)
Transcriptional activation in human cell-free systems containing RNA polymerase II and general initiation factors requires the action of one or more additional coactivators. Here, we report the isolation of cDNAs encoding two novel human transcriptional coactivators (p52 and p75) that
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