Tyrosyl-DNA Phosphodiesterase 2 Recombinant Protein | TDP2 recombinant protein

Recombinant Human Tyrosyl-DNA Phosphodiesterase 2

Cat. Num. AAA146189

• Gene Names: TDP2; EAP2; AD022; EAPII; TTRAP; hTDP2; dJ30M3.3
• Purity: Greater than 85.0% as determined by SDS-PAGE.
• Synonyms: Tyrosyl-DNA Phosphodiesterase 2; Recombinant Human Tyrosyl-DNA Phosphodiesterase 2; TDP2 Human; Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant; AD022; dJ30M3.3; EAP2; EAPII; RP1-30M3.3; TTRAP; 5'-tyrosyl-DNA phosphodiesterase; hTDP2; ETS1-associated protein 2; ETS1-associated protein II; TDP2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 85.0% as determined by SDS-PAGE.
• Form/Format: The TDP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.; Sterile filtered colorless solution.
• Sequence: MGSSHHHHHH SSGLVPRGSH MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL
• Sequence Length: 362

• Preparation and Storage: Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Related Product Information for TDP2 recombinant protein

Description: TDP2 Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Introduction: Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.

Product Categories/Family for TDP2 recombinant protein

Enzymes; Esterase

NCBI and Uniprot Product Information

• NCBI GI #: 23510348
• NCBI GeneID: 51567
• NCBI Accession #: NP_057698.2
• NCBI GenBank Nucleotide #: NM_016614.2
• Molecular Weight: 32,176 Da
• NCBI Official Full Name: tyrosyl-DNA phosphodiesterase 2
• NCBI Official Synonym Full Names: tyrosyl-DNA phosphodiesterase 2
• NCBI Official Symbol: TDP2
• NCBI Official Synonym Symbols: EAP2; AD022; EAPII; TTRAP; hTDP2; dJ30M3.3
• NCBI Protein Information: tyrosyl-DNA phosphodiesterase 2; 5'-Tyr-DNA phosphodiesterase; 5'-tyrosyl-DNA phosphodiesterase; ETS1-associated protein 2; ETS1-associated protein II; TRAF and TNF receptor associated protein; TRAF and TNF receptor-associated protein; VPg unlinkase; tyr-DNA phosphodiesterase 2; tyrosyl-RNA phosphodiesterase
• UniProt Protein Name: Tyrosyl-DNA phosphodiesterase 2
• Protein Family: Tyrosyl-DNA phosphodiesterase
• UniProt Gene Name: TDP2
• UniProt Synonym Gene Names: EAP2; TTRAP; Tyr-DNA phosphodiesterase 2; hTDP2; 5'-Tyr-DNA phosphodiesterase; EAPII
• UniProt Entry Name: TYDP2_HUMAN

NCBI Description

This gene encodes a member of a superfamily of divalent cation-dependent phosphodiesterases. The encoded protein associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. This protein has sequence and structural similarities with APE1 endonuclease, which is involved in both DNA repair and the activation of transcription factors. [provided by RefSeq, Jul 2008]

Uniprot Description

TTRAP: 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. Hydrolyzes 5'- phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. 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 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. Also acts as an adapter by participating to 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. Acts as a regulator of ribosome biogenesis following stress. Belongs to the CCR4/nocturin family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Nucleolus; Inhibitor; EC 3.1.4.-

Chromosomal Location of Human Ortholog: 6p22.3-p22.1

Cellular Component: nucleoplasm; PML body; intercellular bridge; cytoplasm; nucleolus; nucleus

Molecular Function: protein binding; nuclease activity; manganese ion binding; magnesium ion binding; transcription corepressor activity; single-stranded DNA binding

Biological Process: cell surface receptor linked signal transduction; double-strand break repair