Anti-TDP2 / ETS1 associated protein II, clone TDP2/1258

Anti-TDP2 / ETS1 associated protein II, clone TDP2/1258
Item number Size Datasheet Manual SDS Delivery time Quantity Price
NSJ-V3394SAF-100UG 100 µg - -

3 - 10 business days*

810.00€
 
1 mg/ml in 1X PBS, BSA free, sodium azide free. This mAb recognizes a protein of 41kDa, which is... more
Product information "Anti-TDP2 / ETS1 associated protein II, clone TDP2/1258"
1 mg/ml in 1X PBS, BSA free, sodium azide free. This mAb recognizes a protein of 41kDa, which is identified as TDP2, or ETS1 associated protein II. It is 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. 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 also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation. Protein 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. 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. [The UniProt Consortium]
Keywords: Anti-TDP2, Anti-EAP2, Anti-EAPII, Anti-hTDP2, Anti-AD-022, EC=3.1.4.-, Anti-VPg unlinkase, Anti-ETS1-associated protein 2, Anti-ETS1-associated protein II, Anti-Tyr-DNA phosphodiesterase 2, Anti-5'-Tyr-DNA phosphodiesterase, TDP2 Antibody / ETS1 associate
Supplier: NSJ Bioreagents
Supplier-Nr: V3394SAF

Properties

Application: IHC (paraffin), FC, IF
Antibody Type: Monoclonal
Clone: TDP2/1258
Conjugate: No
Host: Mouse
Species reactivity: human
Immunogen: Human recombinant full length protein was used as the immunogen for this TDP2 antibody.
Format: Purified

Handling & Safety

Storage: +4°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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