Recombinant Human PNK/PNKP Protein

Name: Recombinant Human PNK/PNKP Protein
Brand: Beta LifeScience
SKU: BLA-7152P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	Q96T60
Synonym	2''(3'')-polynucleotidase 2'(3')-polynucleotidase Bifunctional polynucleotide phosphatase/kinase DEM 1 DEM1 DNA 5' kinase/3' phosphatase DNA 5''-kinase/3''-phosphatase EIEE10 Homo sapiens polynucleotide kinase 3' phosphatase (PNKP) MCSZ PNK 1 PNK1 Pnkp PNKP DNA kinase PNKP_HUMAN Polynucleotide 3'-phosphatase Polynucleotide 5' hydroxyl kinase Polynucleotide 5''-hydroxyl-kinase Polynucleotide Kinase Polynucleotide kinase 3 prime phosphatase Polynucleotide kinase 3' phosphatase Polynucleotide kinase-3''-phosphatase
Description	Recombinant Human PNK/PNKP Protein was expressed in Wheat germ. It is a Full length protein
Source	Wheat germ
AA Sequence	MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQ VELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLH PLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENL EKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIP RKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVL VATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPG RKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSG PLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRDTLG SWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLF TATLEQARHNNRFREMTDSSHIPVSDMVMYGYRKQFEAPTLAEGFSAILE IPFRLWVEPRLGRLYCQFSEG
Molecular Weight	84 kDa including tags
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.
Subcellular Location	Nucleus. Chromosome.
Protein Families	DNA 3' phosphatase family
Database References	HGNC: 9154 OMIM: 605610 KEGG: hsa:11284 STRING: 9606.ENSP00000323511 UniGene: Hs.78016
Associated Diseases	Microcephaly, seizures, and developmental delay (MCSZ); Ataxia-oculomotor apraxia 4 (AOA4)
Tissue Specificity	Expressed in many tissues with highest expression in spleen and testis, and lowest expression in small intestine. Expressed in higher amount in pancreas, heart and kidney and at lower levels in brain, lung and liver.

Gene Functions References

Despite presence of an alternative 3'-phosphatase, loss of PNKP significantly sensitizes cells to 3'-phosphate-terminated DSBs, due to a 3'-dephosphorylation defect. PMID: 29807321
PNKP mutation in two siblings is associated with progressive ataxia, abnormal saccades, sensorimotor neuropathy and dystonia consistent with ataxia with oculomotor apraxia disorders. PMID: 28552035
we have identified a mutation in PNKP, leading to a phenotype of microcephaly with primordial dwarfism. PMID: 27232581
XRCC1 and PNKP interact via a high-affinity phosphorylation-dependent interaction site in XRCC1 and a forkhead-associated domain in PNKP. Data suggest a second PNKP interaction site in XRCC1 that binds PNKP with lower affinity and independently of XRCC1 phosphorylation. (XRCC1 = X-ray repair cross complementing protein 1; PNKP = polynucleotide kinase 3'-phosphatase) PMID: 28821613
In a recombinant PNKP-XRCC4-LigIV complex, stable binding of PNKP requires XRCC4 phosphorylation. Only one PNKP protomer binds per XRCC4 dimer. Both the PNKP FHA and catalytic domains contact the XRCC4 coiled-coil and LigIV BRCT repeats. A surface on the PNKP phosphatase domain may contact XRCC4-LigIV. A mutation on this surface (E326K) impairs PNKP recruitment to damaged DNA and causes microcephaly with seizures. PMID: 28453785
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). PMID: 27470939
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. PMID: 27125728
In 11 Portuguese patients, PNKP mutations cause ataxia with oculomotor apraxia type 4. PMID: 26970421
Here we report that purified wild-type (WT) ATXN3 stimulates, and by contrast the mutant form specifically inhibits, PNKP's 3' phosphatase activity in vitro. ATXN3-deficient cells also show decreased PNKP activity PMID: 25633985
We now report that the mutant ATXN3 protein interacts with and inactivates PNKP (polynucleotide kinase 3'-phosphatase), an essential DNA strand break repair enzyme PMID: 25590633
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. PMID: 25728773
we show that modest inhibition of PNKP in a PTEN knockout background enhances cellular radiosensitivity, suggesting that such a "synthetic sickness" approach involving the combination of PNKP inhibition with radiotherapy PMID: 23883586
Mutations in PNKP have previously been associated with a syndrome of microcephaly, seizures and developmental delay (MIM 613402), and is now associated with a neurodegenerative disorder. PMID: 23224214
the interaction between PNKP and XRCC1 has roles in the retention of XRCC1 at DNA damage sites and in DNA alkylation damage repair PMID: 22992732
The data suggest that all four known mutations associated with microcephaly, seizures and developmental delay reduce the cellular stability and level of PNKP protein, with three mutations likely ablating cellular DNA 5'-kinase activity and all of the mutations greatly reducing cellular DNA 3'-phosphatase activity. PMID: 22508754
the critical role of NEIL2 and PNKP in maintenance of the mammalian mitochondrial genome. PMID: 22130663
PNKP distorts target DNA structures to access damaged substrate DNA ends, thus providing a molecular mechanism for the involvement of PNKP in the repair of both single- and double-strand breaks. PMID: 22171004
Results reveal that ionizing radiation-induced phosphorylation of PNKP by ATM and DNA-PK regulates PNKP function at DNA double strand breaks. PMID: 21824916
Studies indicate that PNKP serves a crucial role in the repair of DNA strand breaks through interactions with other DNA repair proteins, notably XRCC1 and XRCC4. PMID: 21353781
CK2-mediated phosphorylation of XRCC4 can have different effects on PNKP activity. PMID: 20852255
The neurological abnormalities in individuals with microcephaly, early onset, intractable seizures and develomental delays may reflect a role for PNKP in several DNA repair pathways. PMID: 20118933
Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining PMID: 12032095
First direct physical evidence for ternary complex formation involving a polynucleotide kinase, AMP-PNP, and an oligonucleotide, supports a reaction mechanism in which ATP and DNA bind simultaneously to the enzyme. PMID: 14556639
Data show that polynucleotide kinase is associated with the PARP-1-dependent end-joining pathway, and show functional parallels between the PARP-1 and DNA-PK-dependent end-joining processes. PMID: 16364363
polynucleotide kinase participates in repair of DNA double-strand breaks by nonhomologous end joining but not homologous recombination PMID: 17638872
XRCC1 enhances the capacity of hPNK to discriminate between strand breaks with 5'-OH termini and those with 5'-phosphate termini; and XRCC1 stimulates hPNK activity by displacing hPNK from the phosphorylated DNA product PMID: 17650498
The PNKP T5644G variant does not seem to be involved in adenoma recurrence in the Polyp Prevention Trial. PMID: 18414202
the FHA domain of PNK binds specifically, and with high affinity to a multiply phosphorylated motif in XRCC1 containing a pSer-pThr dipeptide, and forms a 2:1 PNK:XRCC1 complex. PMID: 19155274

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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