Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery
Exalpha Biologicals, Inc.

DNA Topoisomerase 1

  • Product Code: X2732P
  • Size: 100 µg
  • Price (USD): $249

Cat #

X2732P		 Quantity:      

Data Sheet

Product Name

DNA Topoisomerase 1

Host/Source

Rabbit

Isotype

Ig

Product Type

Antigen Immunoaffinity Purified Polyclonal

Reactivity

Human

Applications

Immunohistochemistry (paraffin-embedded)

Purification

Antigen Immunoaffinity Purification

Size

100 µg

Price (USD)

$249

Background

DNA Topoisomerase 1 releases the supercoiling and torsional tension of DNA introduced during DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. It introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.

Immunogen

Synthetic peptide made to human DNA Topoisomerase 1

Positive Control

Found in Endothelial cells.

Formulation

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Customer Storage

Product should be stored at -20ºC. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

90.7 kDa

Product Image

Image Legend

Immunohistochemical staining of normal human tonsil tissue using TOP1 antibody (Cat. No. X2732P) at 10 µg/ml and detected using anti-Rabbit HRP secondary antibody and visualized using DAB substrate and hematoxylin counterstain.

Database Links:

SwissProtP11387Human

References

1. Oddou, P., et al. 'Monoclonal antibodies neutralizing mammalian DNA topoisomerase I activity.' Eur. J. Biochem. 1988, 177, 523-529 2. Redinbo, M.R., et al. 'Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA.' Biochemistry 2000, 39, 6832-6840 3. Eisenreich, A., et al. 'Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells.' Circ. Res. 2009, 104, 589-599