| Product Name | TDP1, 1-608aa, Human, Baculovirus |
|---|---|
| Description | TDP1, also known as tyrosyl-DNA phosphodiesterase 1, is involved in repairing stalled topoisomerase l-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase l and the 3-prime phosphate of DNA. This protein may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical meditated DNA double-strand breaks. Recombinant human TDP1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Synonyms | tyrosyl-DNA phosphodiesterase 1 isoform a, TDP1, Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1 |
| Host | Virus |
| Molecular Weight | 19.6 kDa (169 aa) |
| Amino Acid Sequence | ADPMSQEGDY GRWTISSSDE SEEEKPKPDK PSTSSLLCAR QGAANEPRYT CSEAQKAAHK RKISPVKFSN TDSVLPPKRQ KSGSQEDLGW CLSSSDDELQ PEMPQKQAEK VVIKKEKDIS APNDGTAQRT ENHGAPACHR LKEEEDEYET SGEGQDIWDM LDKGNPFQFY LTRVSGVKPK YNSGALHIKD ILSPLFGTLV SSAQFNYCFD VDWLVKQYPP EFRKKPILLV HGDKREAKAH LHAQAKPYEN ISLCQAKLDI AFGTHHTKMM LLLYEEGLRV VIHTSNLIHA DWHQKTQGIW LSPLYPRIAD GTHKSGESPT HFKADLISYL MAYNAPSLKE WIDVIHKHDL SETNVYLIGS TPGRFQGSQK DNWGHFRLKK LLKDHASSMP NAESWPVVGQ FSSVGSLGAD ESKWLCSEFK ESMLTLGKES KTPGKSSVPL YLIYPSVENV RTSLEGYPAG GSLPYSIQTA EKQNWLHSYF HKWSAETSGR SNAMPHIKTY MRPSPDFSKI AWFLVTSANL SKAAWGALEK NGTQLMIRSY ELGVLFLPSA FGLDSFKVKQ KFFAGSQEPM ATFPVPYDLP PELYGSKDRP WIWNIPYVKA PDTHGNMWVP SHHHHHH |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20 mM Tris-HCl buffer (pH 7.5) containing 300 mM NaCl, 0.1 mM DTT, 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Jakobsen AK., et al, (2015) Exp. Mol. Pathol. 99:56-64. Lebedeva NA., et al, (2015) Biosci. Rep. 35:e00230. |
| Background | TDP1, also known as tyrosyl-DNA phosphodiesterase 1, is involved in repairing stalled topoisomerase l-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase l and the 3-prime phosphate of DNA. This protein may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical meditated DNA double-strand breaks. Recombinant human TDP1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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