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anti-Mouse (Murine) PNKP Antikörper:
anti-Human PNKP Antikörper:
anti-Rat (Rattus) PNKP Antikörper:
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Human Polyclonal PNKP Primary Antibody für ELISA - ABIN249588
Jilani, Ramotar, Slack, Ong, Yang, Scherer, Lasko: Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3'-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage. in The Journal of biological chemistry 1999
Human Polyclonal PNKP Primary Antibody für ICC, IF - ABIN4346526
Shimada, Dumitrache, Russell, McKinnon: Polynucleotide kinase-phosphatase enables neurogenesis via multiple DNA repair pathways to maintain genome stability. in The EMBO journal 2015
The work indicates that the phosphatase domain of Pnkp binds 3'-phosphorylated single-stranded DNAs in a manner that is highly dependent on the presence of the 3'-phosphate.
Directed postnatal neural inactivation of PNKP affected specific subpopulations including oligodendrocytes, indicating a broad requirement for genome maintenance, both during and after neurogenesis.
Structure of dsDNA bound to PNK 5'-kinase domain reveals DNA bending facilitating recognition of DNA ends in the context of single-strand/double-strand breaks, suggesting close functional cooperation in between the kinase/phosphatase active sites.
we have identified a mutation in PNKP, leading to a phenotype of microcephaly with primordial dwarfism.
XRCC1 (zeige XRCC1 Antikörper) and PNKP interact via a high-affinity phosphorylation-dependent interaction site in XRCC1 (zeige XRCC1 Antikörper) and a forkhead-associated domain in PNKP. Data suggest a second PNKP interaction site in XRCC1 (zeige XRCC1 Antikörper) that binds PNKP with lower affinity and independently of XRCC1 (zeige XRCC1 Antikörper) phosphorylation. (XRCC1 (zeige XRCC1 Antikörper) = X-ray repair cross complementing protein 1 (zeige XRCC1 Antikörper); PNKP = polynucleotide kinase 3'-phosphatase)
In a recombinant PNKP-XRCC4 (zeige XRCC4 Antikörper)-LigIV complex, stable binding of PNKP requires XRCC4 (zeige XRCC4 Antikörper) phosphorylation. Only one PNKP protomer binds per XRCC4 (zeige XRCC4 Antikörper) dimer. Both the PNKP FHA (zeige CRY2 Antikörper) and catalytic domains contact the XRCC4 (zeige XRCC4 Antikörper) coiled-coil and LigIV BRCT repeats. A surface on the PNKP phosphatase domain may contact XRCC4 (zeige XRCC4 Antikörper)-LigIV. A mutation on this surface (E326K) impairs PNKP recruitment to damaged DNA and causes microcephaly with seizures.
Mutations in TDP1 and APTX have been linked to Spinocerebellar ataxia with axonal neuropathy (SCAN1) and Ataxia-ocular motor apraxia 1 (AOA1), respectively, while mutations in PNKP are considered to be responsible for Microcephaly with seizures (MCSZ) and Ataxia-ocular motor apraxia 4 (AOA4).
the role for PNKP in maintaining brain function and how perturbation in its activity can account for the varied pathology of neurodegeneration or microcephaly present in microcephaly with seizures and ataxia with oculomotor apraxia 4 respectively.
In 11 Portuguese patients, PNKP mutations cause ataxia with oculomotor apraxia type 4.
Here we report that purified wild-type (WT) ATXN3 (zeige ATXN3 Antikörper) stimulates, and by contrast the mutant form specifically inhibits, PNKP's 3' phosphatase activity in vitro. ATXN3 (zeige ATXN3 Antikörper)-deficient cells also show decreased PNKP activity
We now report that the mutant ATXN3 (zeige ATXN3 Antikörper) protein interacts with and inactivates PNKP (polynucleotide kinase 3'-phosphatase), an essential DNA strand break repair enzyme
We identified homozygous or compound-heterozygous PNKP mutations in eight of the nine Portuguese families we studied, suggesting that, in Portugal, mutations in PNKP are the most frequent cause of ataxia with oculomotor apraxia.
we show that modest inhibition of PNKP in a PTEN (zeige PTEN Antikörper) knockout background enhances cellular radiosensitivity, suggesting that such a "synthetic sickness" approach involving the combination of PNKP inhibition with radiotherapy
The protein encoded by this gene phosphorylates vitamin B6, a step required for the conversion of vitamin B6 to pyridoxal-5-phosphate, an important cofactor in intermediary metabolism. The encoded protein is cytoplasmic and probably acts as a homodimer. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.
polynucleotide kinase 3'-phosphatase
, DNA 5'-kinase/3'-phosphatase
, bifunctional polynucleotide phosphatase/kinase
, polynucleotide kinase-3'-phosphatase
, Homo sapiens polynucleotide kinase 3'-phosphatase (PNKP)
, pyridoxal kinase
, pyridoxamine kinase
, pyridoxine kinase
, vitamin B6 kinase