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Topoisomerase 3 beta1 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IP, IHC-P, E |
|---|---|
| Primary Accession | O95985 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 100 KDa |
| Gene ID | 8940 |
|---|---|
| Other Names | DNA topoisomerase 3-beta-1, DNA topoisomerase III beta-1, TOP3B, TOP3B1 |
| Target/Specificity | KLH-conjugated synthetic peptide encompassing a sequence within the N-term region of human Topoisomerase 3 beta1. The exact sequence is proprietary. |
| Dilution | WB~~1:1000 IP~~N/A IHC-P~~N/A E~~N/A |
| Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | TOP3B |
|---|---|
| Synonyms | TOP3B1 |
| Function | Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. 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-(5'-phosphotyrosyl)- enzyme intermediate and the expulsion of a 3'-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 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity. |
| Tissue Location | Isoform 1 is found in testis, heart and skeletal muscle. A 4 kb transcript which probably represents isoform 2 is found in thymus, kidney and pancreas. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. 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-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-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 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity.
References
Ng S.-W.,et al.Nucleic Acids Res. 27:993-1000(1999).
Kawasaki K.,et al.Genome Res. 7:250-261(1997).
Hanai R.,et al.Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
Riou J.F.,et al.Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
Collins J.E.,et al.Genome Biol. 5:R84.1-R84.11(2004).
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