产品名称
Topo I (N1-197) (NTD) human, recombinant, expressed in insect cells, ≥85% (SDS-PAGE)
biological source
human
recombinant
expressed in insect cells
assay
≥85% (SDS-PAGE)
form
frozen liquid
mol wt
~25.3 kDa
packaging
pkg of 5 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
1000 μg/mL
color
clear colorless
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... TOP1(7150)
Biochem/physiol Actions
Human DNA topoisomerase I is the best studied of the DNA topoisomerase family. It catalyzes the relaxation of both positive and negative supercoils without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA topoisomerase I also plays a major role in pre-mRNA splicing, cell cycle and other gene regulatory pathways during cell growth and development. The N-terminal 214 amino acids of topoisomerase I comprise a highly charged N-terminal domain (NTD) involved in protein-protein interactions with a number of cellular proteins, including SV40 T antigen, nucleolin, SR proteins, p53 and other transcription factors.
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
D Gai et al.
Journal of virology, 74(11), 5224-5232 (2000-05-09)
Topoisomerase I (topo I) is required for releasing torsional stress during simian virus 40 (SV40) DNA replication. Recently, it has been demonstrated that topo I participates in initiation of replication as well as in elongation. Although T antigen and topo
P Haluska et al.
Nucleic acids research, 26(7), 1841-1847 (1998-05-30)
We have attempted to identify human topoisomerase I-binding proteins in order to gain information regarding the cellular roles of this protein and the cytotoxic mechanisms of the anticancer drug camptothecin, which specifically targets topoisomerase I. In the course of this
Yinghui Mao et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(3), 1235-1240 (2002-01-24)
The nonconserved, hydrophilic N-terminal domain of eukaryotic DNA topoisomerase I (topo I) is dispensable for catalytic activity in vitro but essential in vivo. There are at least five putative nuclear localization signals and a nucleolin-binding signal within the first 215
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