Bifunctional polynucleotide phosphatase/kinase Recombinant Protein | PNKP recombinant protein

Recombinant Human Bifunctional polynucleotide phosphatase/kinase

Cat. Num. AAA1298034

• Gene Names: PNKP; PNK; AOA4; MCSZ; EIEE10
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Bifunctional polynucleotide phosphatase/kinase; Recombinant Human Bifunctional polynucleotide phosphatase/kinase; DNA 5'-kinase/3'-phosphatase; Polynucleotide kinase-3'-phosphatase; Including the following 2 domains; Polynucleotide 3'-phosphatase; EC=3.1.3.32; 2'(3')-polynucleotidase; Polynucleotide 5'-hydroxyl-kinase (EC:2.7.1.78); PNKP recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-521aa; Full Length
• Sequence: MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVLVATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPGRKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSGPLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRDTLGSWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLFTATLEQARHNNRFREMTDSSHIPVSDMVMYGYRKQFEAPTLAEGFSAILEIPFRLWVEPRLGRLYCQFSEG

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for PNKP recombinant protein

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 roving 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.

Product Categories/Family for PNKP recombinant protein

Epigenetics and Nuclear Signaling

References

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.Jilani A., Ramotar D., Slack C., Ong C., Yang X.M., Scherer S.W., Lasko D.D.J. Biol. Chem. 274:24176-24186(1999) Molecular characterization of a human DNA kinase.Karimi-Busheri F., Daly G., Robins P., Canas B., Pappin D.J.C., Sgouros J., Miller G.G., Fakhrai H., Davis E.M., Le Beau M.M., Weinfeld M.J. Biol. Chem. 274:24187-24194(1999) Cloning a cDNA which is differently expressed in malignancies.Yang H.W., Piao H.Y., Chen Y.Z., Hayashi Y.Genomic organization, physical mapping and expression analysis of the human polynucleotide kinase-3'-phosphatase (PNKP) gene.Scorilas A., Katsaros N.NIEHS SNPs programThe DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK.Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.Nucleic Acids Res. 37:1701-1712(2009) Mutations in PNKP cause microcephaly, seizures and defects in DNA repair.Shen J., Gilmore E.C., Marshall C.A., Haddadin M., Reynolds J.J., Eyaid W., Bodell A., Barry B., Gleason D., Allen K., Ganesh V.S., Chang B.S., Grix A., Hill R.S., Topcu M., Caldecott K.W., Barkovich A.J., Walsh C.A.Nat. Genet. 42:245-249(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 31543419
• NCBI GeneID: 11284
• NCBI Accession #: NP_009185.2
• NCBI GenBank Nucleotide #: NM_007254.3
• UniProt Accession #: Q96T60; Q9BUL2; Q9P1V2; Q9UKU8; Q9UNF8; Q9UNI0
• Molecular Weight: 73.1 kDa
• NCBI Official Full Name: bifunctional polynucleotide phosphatase/kinase
• NCBI Official Synonym Full Names: polynucleotide kinase 3'-phosphatase
• NCBI Official Symbol: PNKP
• NCBI Official Synonym Symbols: PNK; AOA4; MCSZ; EIEE10
• NCBI Protein Information: bifunctional polynucleotide phosphatase/kinase
• UniProt Protein Name: Bifunctional polynucleotide phosphatase/kinase
• Protein Family: Bifunctional polynucleotide phosphatase/kinase
• UniProt Gene Name: PNKP
• UniProt Entry Name: PNKP_HUMAN

NCBI Description

This locus represents a gene involved in DNA repair. In response to ionizing radiation or oxidative damage, the protein encoded by this locus catalyzes 5' phosphorylation and 3' dephosphorylation of nucleic acids. Mutations at this locus have been associated with microcephaly, seizures, and developmental delay.[provided by RefSeq, Sep 2010]

Uniprot Description

Pnk1: polynucleotide kinase 3'-phosphatase. May be involved in double-strand break repair by non-homologous end joining. Required for normal response to DNA damage by gamma-radiation or camptothecin in S. pombe.

Protein type: EC 2.7.1.78; EC 3.1.3.32; DNA-binding; Phosphatase (non-protein); Kinase, other

Chromosomal Location of Human Ortholog: 19q13.3-q13.4

Cellular Component: membrane; nucleolus; nucleoplasm; nucleus

Molecular Function: ATP binding; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; damaged DNA binding; double-stranded DNA binding; endonuclease activity; nucleotide kinase activity; polynucleotide 3'-phosphatase activity; protein binding; purine nucleotide binding

Biological Process: base-excision repair; dephosphorylation; DNA damage response, detection of DNA damage; DNA repair; DNA-dependent DNA replication; nucleotide phosphorylation; nucleotide-excision repair, DNA damage removal; positive regulation of telomerase activity; positive regulation of telomere maintenance via telomerase; response to oxidative stress; response to radiation

Disease: Ataxia-oculomotor Apraxia 4; Microcephaly, Seizures, And Developmental Delay