Recombinant Human Tyrosyl-DNA phosphodiesterase 1 (TDP1)

Code CSB-YP023352HU
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP023352HU
MSDS
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP023352HU-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP023352HU
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP023352HU
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
TDP1
Uniprot No.
Alternative Names
AI838772; AW493413; FLJ11090; MGC104252; MGC112732; RP24-311F12.2; SCAN1; TDP1; TYDP; TYDP1_HUMAN; Tyr-DNA phosphodiesterase 1; Tyrosyl-DNA phosphodiesterase 1
Species
Homo sapiens (Human)
Expression Region
1-608
Target Protein Sequence
MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGIWLSP LYPRIADGTH KSGESPTHFK ADLISYLMAY NAPSLKEWID VIHKHDLSET NVYLIGSTPG RFQGSQKDNW GHFRLKKLLK DHASSMPNAE SWPVVGQFSS VGSLGADESK WLCSEFKESM LTLGKESKTP GKSSVPLYLI YPSVENVRTS LEGYPAGGSL PYSIQTAEKQ NWLHSYFHKW SAETSGRSNA MPHIKTYMRP SPDFSKIAWF LVTSANLSKA AWGALEKNGT QLMIRSYELG VLFLPSAFGL DSFKVKQKFF AGSQEPMATF PVPYDLPPEL YGSKDRPWIW NIPYVKAPDT HGNMWVPS
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate.
Gene References into Functions
  1. The role of conserved residues Y204, F259, S400 and W590 of the catalytic groove of TDP1 protein DNA cleavage activity was analyzed. PMID: 29747024
  2. We found the rs942190 GG genotype of TDP1 to be associated with relatively poor survival among small-cell lung cancer patients. Further investigation is needed to confirm the result and to determine whether this genotype may be a predictive marker for treatment efficacy of DNA topoisomerase inhibitors PMID: 28974547
  3. this study identifies the importance of TDP1 as a novel determinant of response to CNDAC across various cancer types (especially non-small cell lung cancers), and demonstrates the differential involvement of BRCA2, PARP1, and TDP1 in the cellular responses to CNDAC, AraC, and CPT PMID: 28802254
  4. Data indicate that the initial step of tyrosyl-DNA phosphodiesterase 1 (Tdp1) interaction with DNA includes binding of Tdp1 to the DNA ends followed by the 3'-nucleosidase reaction. PMID: 27687298
  5. Data indicate a molecular basis for DNA 3'-end processing by tyrosyl-DNA phosphodiesterase (Tdp1). PMID: 29295983
  6. Expression of human Tdp1HisnucAla and Tdp1HisgabAsn mutants results in stabilization of the covalent TDP1-DNA intermediate and induces cytotoxicity. PMID: 27893431
  7. We show that two genes, TDP1, a tyrosyl-DNA-phosphdiesterase, and TAF12, an RNA polymerase II TATA-box binding factor, cause CIN when overexpressed in human cells. Using SDL screens in yeast, we identified a set of genes that when deleted specifically kill cells with high levels of Tdp1 PMID: 27551064
  8. TDP1 participation in human non-homologous end joining (NHEJ) is mediated by interaction with XLF, and that TDP1-XLF interactions and subsequent NHEJ events are regulated by phosphorylation of TDP1-S81. PMID: 29078113
  9. The data obtained suggest that PARP1 and TDP1 bind in an antiparallel orientation; the N-terminus of the former protein interacts with the C-terminal domain of the latter. PMID: 26181362
  10. Tyrosyl-DNA-phosphodiesterase I (TDP1) participates in the removal and repair of stabilized-Top2alpha cleavage complexes in human cells. PMID: 26421495
  11. varying expression levels of TOP1 and TDP1 polypeptides in multiple colorectal cancer cell lines and in clinical colorectal cancer samples, are reported. PMID: 25522766
  12. both TOP1 and TDP1 were upregulated in the tumor tissue compared to the adjacent non-tumor tissue in non-small cell lung cancer tissue PMID: 25987486
  13. Density functional theory computations are used to acquire thermodynamic and kinetic data along the catalytic pathway, including the phosphoryl transfers of Tdp1 and subsequent hydrolysis. PMID: 26121557
  14. TDP1 plays a role during the early stages of mammalian NHEJ. TPD1 stimulated DNA binding by XLF. TDP1 also promoted DNA binding by Ku70/80 and stimulated DNA-PK activity. PMID: 25841101
  15. These findings suggest that the flexibility of Tdp1 active site residues may impair the resolution of mutant Tdp1 covalent phosphohistidyl intermediates PMID: 25609251
  16. This article summarizes and compares the biochemistry, functions, and post-translational regulation of TDP1 and TDP2, as well as the relevance of TDP1 and TDP2 as determinants of response to anticancer agents PMID: 24856239
  17. Data provides insights into the possible inactivation of TDP1 in cancers and its relationship to cellular response to Top1-targeted drugs. PMID: 24355542
  18. Results show Tdp1 catalyzes hydrolysis of apurinic/apyrimidinic site analog correlates with the DNA helix distortion induced by the substituent. PMID: 24183900
  19. marked overexpression of TDP1 protein and mRNA in rhabdomyosarcoma tumors was observed; results suggest a compensatory role for TDP1 in rhabdomyosarcoma after topoisomerase-I based therapy PMID: 23913164
  20. TDP1 deficiency sensitizes human cells to base damage, independently of apurinic/apyrimidinic endonuclease I (APE1). PMID: 24335147
  21. These studies suggest that one role of cytoplasmic Tdp1 is the repair of mitochondrial DNA lesions arising from oxidative stress. PMID: 23536040
  22. A polymorphism at position rs28365054 in the TDP1 gene had a significant difference (P < 0.05) in the genotype distributions between the Tourette syndrome patients and the control group PMID: 23852793
  23. study identifies TDP1 as a target for modification by the small ubiquitin-like modifier SUMO and provides evidence implicating SUMOylation in facilitating TDP1 cellular function during single-strand break repair PMID: 22415824
  24. Our findings reveal a broad involvement of Tdp1 in DNA repair and clarify the role of human TDP1 in the repair of Top2-induced DNA damage. PMID: 22375014
  25. Analysis of the active-site mechanism of tyrosyl-DNA phosphodiesterase I. PMID: 22155078
  26. topoisomerase 1, tyrosyl-DNA phosphodiesterase 1, and single-strand break repair modulate transcription-dependent CAG repeat contractions PMID: 21628532
  27. Study investigates substrate specificity of Tdp1; data suggest a role for Tdp1 in a new APE-independent base excision repair pathway. PMID: 21276450
  28. These findings provide evidence for TDP1 as a novel mitochondrial enzyme. PMID: 21041670
  29. results suggest human Tdp1 may act using a scanning mechanism, in which Tdp1 bind non-specifically upstream of a 3'-blocking lesion and is preferentially stabilized at 3'-DNA ends corresponding to its site of action. PMID: 20097655
  30. The interaction with Lig3alpha is promoted by serine 81 that is located within a putative S/TQ site in the N-terminus domain of TDP1. PMID: 20009512
  31. TDP1 phosphorylation at serine residue 81 promotes cell survival and DNA repair in response to carnitine O-palmitoyltransferase-induced DNA double-strand breaks. PMID: 19851285
  32. 1.69 A crystal structure of human tyrosyl-DNA phosphodiesterase PMID: 11839309
  33. a role for hTdp1 in repair of free radical-mediated DNA double strand breaks bearing terminally blocked 3' overhangs. PMID: 12023295
  34. loss-of-function mutations in TDP1 may cause spinocerebellar ataxia with axonal neuropathy either by interfering with DNA transcription or by inducing apoptosis in postmitotic neurons PMID: 12244316
  35. We report the three-dimensional structures of human Tdp1 bound to the phosphate transition state analogs vanadate and tungstate PMID: 12470949
  36. conserved sequences and amino acids important for catalytic activity and enzyme specificity were identified PMID: 15248776
  37. TDP1 is required for the repair of topoisomerase I-mediated DNA damage and may have a role in the repair of DNA damage mediated by topoisomerase II PMID: 15494395
  38. The role of TDP1 in 3'-phosphoglycolate processing during in vitro end joining of DNA double-strand breaks. PMID: 15647511
  39. Tdp1 only acts upon double strand breaks in vivo PMID: 15811850
  40. inhibitors of Tdp1 could act synergistically with camptothecin in anticancer therapy PMID: 15920477
  41. Tdp1 may function to remove a variety of 3' adducts from DNA during DNA repair PMID: 16141202
  42. TDP1 has a role in DNA single-strand break repair and neurodegeneration [review] PMID: 16775218
  43. it is proposed that Tdp1 is involved in the repair of Top1 cleavage complexes associated with transcription damage in hereditary spinocerebellar ataxia with axonal neuropathy (SCAN1) cells PMID: 16935573
  44. TDP1 is also required for the repair of single stranded breaks induced by ionizing radiation (IR), though not measurably for IR-induced DNA double-strand breaks PMID: 17600775
  45. Data show that mutation of a conserved active site residue converts tyrosyl-DNA phosphodiesterase I into a DNA topoisomerase I-dependent poison. PMID: 17707402
  46. This study provides a direct demonstration that Tdp1 repairs Topo I covalent lesions in vivo and suggests that spinocerebellar ataxia with axonal neuropathy (SCAN1) arises from the recessive neomorphic mutation H493R. PMID: 17948061
  47. TDP1 can gain access to and can process blocked 3' termini of double-strand breaks before ends are fully sequestered by DNA-PK, as well as at a later stage after DNA-PK autophosphorylation. PMID: 19505854
  48. Sequences nearly identical to FLJ11090 are highly homologous to the yeast TDP1 gene. Tdp1 protein cleaves the linkage between a phosphotyrosyl group and the 3'-end of DNA, and has been shown to be involved in the repair of TOP1-induced DNA damage. PMID: 10521354
  49. Protein assay of expressed FLJ11090 shows that it encodes human tyrosyl-DNA phodphodiesterase (TDP1). PMID: 11572945

Show More

Hide All

Involvement in disease
Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy (SCAN1)
Subcellular Location
Nucleus. Cytoplasm.
Protein Families
Tyrosyl-DNA phosphodiesterase family
Tissue Specificity
Ubiquitously expressed. Similar expression throughout the central nervous system (whole brain, amygdala, caudate nucleus, cerebellum, cerebral cortex, frontal lobe, hippocampus, medulla oblongata, occipital lobe, putamen, substantia nigra, temporal lobe,
Database Links

HGNC: 18884

OMIM: 607198

KEGG: hsa:55775

STRING: 9606.ENSP00000337353

UniGene: Hs.209945

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1