m7GpppN-mRNA hydrolase Recombinant Protein | DCP2 recombinant protein

Recombinant Human m7GpppN-mRNA hydrolase

Cat. Num. AAA1310963

• Gene Names: DCP2; NUDT20
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: m7GpppN-mRNA hydrolase; Recombinant Human m7GpppN-mRNA hydrolase; Nucleoside diphosphate-linked moiety X motif 20; Nudix motif 20m; RNA-decapping enzyme 2; hDpc; DCP2 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: 1-385. Full Length of Isoform 2
• Sequence: METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL

• 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 DCP2 recombinant protein

Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Roves the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety

Product Categories/Family for DCP2 recombinant protein

Transcription

References

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Genet. 36:40-45(2004) The DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Human Dcp2 a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures.van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Seraphin B.EMBO J. 21:6915-6924(2002) The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.RNA 8:1489-1501(2002) Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities.Lejeune F., Li X., Maquat L.E.Mol. Cell 12:675-687(2003) Functional characterization of the mammalian mRNA decapping enzyme hDcp2.Piccirillo C., Khanna R., Kiledjian M.RNA 9:1138-1147(2003) A protein interaction framework for human mRNA degradation.Lehner B., Sanderson C.M.Genome Res. 14:1315-1323(2004) Cytoplasmic foci are sites of mRNA decay in human cells.Cougot N., Babajko S., Seraphin B.J. Cell Biol. 165:31-40(2004) Functional analysis of mRNA scavenger decapping enzymes.Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.RNA 10:1412-1422(2004) Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping.Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.Mol. 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Commun. 370:195-199(2008) Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'.Mullen T.E., Marzluff W.F.Genes Dev. 22:50-65(2008) 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) 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) Multiple mRNA decapping enzymes in mammalian cells.Song M.G., Li Y., Kiledjian M.Mol. 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NCBI and Uniprot Product Information

• NCBI GI #: 334688848
• NCBI GeneID: 167227
• NCBI Accession #: NP_001229306.1
• NCBI GenBank Nucleotide #: NM_001242377.1
• UniProt Accession #: Q8IU60; Q6P2D4; Q7Z5W5; Q8NBG5; C9J778
• Molecular Weight: 46.4 kDa
• NCBI Official Full Name: m7GpppN-mRNA hydrolase isoform 2
• NCBI Official Synonym Full Names: decapping mRNA 2
• NCBI Official Symbol: DCP2
• NCBI Official Synonym Symbols: NUDT20
• NCBI Protein Information: m7GpppN-mRNA hydrolase
• UniProt Protein Name: m7GpppN-mRNA hydrolase
• Protein Family: mRNA-decapping enzyme
• UniProt Gene Name: DCP2
• UniProt Synonym Gene Names: NUDT20; Nudix motif 20; hDpc
• UniProt Entry Name: DCP2_HUMAN

NCBI Description

The protein encoded by this gene is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It removes the 7-methyl guanine cap structure from mRNA, prior to its degradation from the 5' end. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.[provided by RefSeq, Jun 2011]

Uniprot Description

DCP2: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Removes the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety. Belongs to the Nudix hydrolase family. DCP2 subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: RNA processing; EC 3.6.1.62; Hydrolase

Chromosomal Location of Human Ortholog: 5q22.2

Cellular Component: cell junction; cytosol; intracellular membrane-bound organelle; nucleoplasm

Molecular Function: exoribonuclease activity, producing 5'-phosphomonoesters; m7G(5')pppN diphosphatase activity; manganese ion binding; protein binding; RNA binding

Biological Process: deadenylation-dependent decapping; gene expression; mRNA catabolic process; mRNA catabolic process, deadenylation-dependent decay; mRNA catabolic process, nonsense-mediated decay; regulation of mRNA stability