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AB140722

Recombinant Human TDP2 protein

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Recombinant Human TDP2 protein is a Human Full Length protein, in the 1 to 362 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

EAP2, TTRAP, AD-022, TDP2, Tyrosyl-DNA phosphodiesterase 2, Tyr-DNA phosphodiesterase 2, hTDP2, 5'-tyrosyl-DNA phosphodiesterase, ETS1-associated protein 2, ETS1-associated protein II, TRAF and TNF receptor-associated protein, Tyrosyl-RNA phosphodiesterase, VPg unlinkase, 5'-Tyr-DNA phosphodiesterase, EAPII

1 Images
SDS-PAGE - Recombinant Human TDP2 protein (AB140722)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human TDP2 protein (AB140722)

3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

O95551

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSMELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKISPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFLQEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFPSTKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQEAPESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQMNSNLGITAACKLRFDRIFFRAAAEEGHIIPRSLDLLGLEKLDCGRFPSDHWGLLCNLDIIL","proteinLength":"Full Length","predictedMolecularWeight":"43.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":362,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O95551","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TDP2 also known as Tyrosyl-DNA phosphodiesterase 2 functions mechanically by repairing DNA through removing topoisomerase II-DNA adducts. It has a mass of approximately 53 kDa. TDP2 shows expression in various tissues with notable levels in brain and muscle. The enzyme exhibits phosphodiesterase activity which is essential for resolving stalled topoisomerase-2-mediated breaks during the repair process.
Biological function summary

TDP2 plays an important role in DNA repair mechanisms. It participates in excising 5'-phosphotyrosyl moieties linked to DNAn important for maintaining genomic stability. TDP2 does not work as a part of a large protein complex but its activity supports several cellular processes by ensuring proper DNA repair. It facilitates the release of covalent protein-DNA complexes therefore aiding cell survival and function.

Pathways

TDP2 contributes to the DNA damage response and repair pathways. It acts in concert with proteins like XRCC1 and PARP1 to ensure repair of DNA strand breaks. Additionally TDP2 is involved in the non-homologous end joining (NHEJ) pathway an important mechanism for repairing double-strand breaks. Its function complements topoisomerase-related activities maintaining genomic integrity during cell division.

TDP2 has been connected to neurodegenerative diseases and certain cancers. Mutations or dysfunctions in TDP2 can lead to spinocerebellar ataxia and intellectual disability as the enzyme’s role in DNA repair is compromised. In cancer disruptions in TDP2 activity can influence cancer progression with interactions involving proteins like ATM playing a role in oncogenesis. Understanding these relationships highlights potential therapeutic targets for treatment strategies.
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Specifications

Form

Liquid

Additional notes

ab140722 is purified using conventional chromatography techniques.

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General info

Function

DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation (PubMed : 27060144, PubMed : 27099339). Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Acts as a regulator of ribosome biogenesis following stress. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta : associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation.. (Microbial infection) Also acts as a 5'-tyrosyl-RNA phosphodiesterase following picornavirus infection : its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA.

Sequence similarities

Belongs to the CCR4/nocturin family.

Post-translational modifications

Ubiquitinated by TRAF6.

Subcellular localisation

Nucleus

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Product protocols

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Target data

DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation (PubMed : 27060144, PubMed : 27099339). Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Acts as a regulator of ribosome biogenesis following stress. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta : associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation.. (Microbial infection) Also acts as a 5'-tyrosyl-RNA phosphodiesterase following picornavirus infection : its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA.
See full target information TDP2
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