Polyadenylate-binding protein 1 Recombinant Protein | PABPC1 recombinant protein

Recombinant Human Polyadenylate-binding protein 1

Cat. Num. AAA960232

• Gene Names: PABPC1; PAB1; PABP; PABP1; PABPC2; PABPL1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Polyadenylate-binding protein 1; Recombinant Human Polyadenylate-binding protein 1; PABPC1 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: 1-370aa; Partial
• Sequence: MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQR

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• 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 PABPC1 recombinant protein

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing prature stop codons; for the recognition of prature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.

Product Categories/Family for PABPC1 recombinant protein

Epigenetics and Nuclear Signaling

References

Human mRNA polyadenylate binding protein evolutionary conservation of a nucleic acid binding motif.Grange T., de Sa C.M., Oddos J., Pictet R.Nucleic Acids Res. 15:4771-4787(1987) The human poly(A) -binding protein (PABP) gene structural and functional analysis.Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O. DNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006) Nucleotide sequence of a partial cDNA encoding a novel human polyadenylate-binding protein.Murphy E.P., McKenna N.J., Headon D.R.Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.Submitted (DEC-2008) to UniProtKB Bienvenut W.V., Waridel P., Quadroni M.Submitted (MAR-2009) to UniProtKB The mRNA poly(A) -binding protein localization, abundance, and RNA-binding specificity.Goerlach M., Burd C.G., Dreyfuss G.Exp. Cell Res. 211:400-407(1994) The human poly(A) -binding protein 1 shuttles between the nucleus and the cytoplasm.Afonina E., Stauber R., Pavlakis G.N.J. Biol. Chem. 273:13015-13021(1998) Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation.Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.Nature 392:520-523(1998) A mechanism for translationally coupled mRNA turnover interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.Cell 103:29-40(2000) Translational repression by a novel partner of human poly(A) binding protein, Paip2.Khaleghpour K., Svitkin Y.V., Craig A.W.B., De;Maria C.T., Deo R.C., Burley S.K., Sonenberg N.Mol. Cell 7:205-216(2001) Dual interactions of the translational repressor Paip2 with poly(A) binding protein.Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N.Mol. Cell. Biol. 21:5200-5213(2001) PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.Lee J., Bedford M.T.EMBO Rep. 3:268-273(2002) Paip1 interacts with poly(A) binding protein through two independent binding motifs.Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N.Mol. Cell. Biol. 22:3769-3782(2002) Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.RNA 8:426-439(2002) Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization.Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.Biochem. Biophys. Res. Commun. 301:665-670(2003) UNR, a new partner of poly(A) -binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant.Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.Genes Dev. 18:2010-2023(2004) The autoregulatory translational control element of poly(A) -binding protein mRNA forms a heteromeric ribonucleoprotein complex.Patel G.P., Ma S., Bag J.Nucleic Acids Res. 33:7074-7089(2005) IMP1 interacts with poly(A) -binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain.Patel G.P., Bag J.FEBS J. 273:5678-5690(2006) Regulation of poly(A) binding protein function in translation Characterization of the Paip2 homolog, Paip2B.Berlanga J.J., Baass A., Sonenberg N.RNA 12:1556-1568(2006) Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells.Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.EMBO Rep. 8:1052-1060(2007) NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells.Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.J. Virol. 81:3786-3796(2007) Molecular composition of IMP1 ribonucleoprotein granules.Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.Mol. Cell. Proteomics 6:798-811(2007) Nuclear localization of cytoplasmic poly(A) -binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN.Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.J. Virol. 82:11283-11293(2008) A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay.Singh G., Rebbapragada I., Lykke-Andersen J.PLoS Biol. 6:E111-E111(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) 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) Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.RNA 15:104-115(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Poly(A) -binding protein (PABP) a common viral target.Smith R.W., Gray N.K.Biochem. J. 426:1-12(2010) The RNA binding protein Larp1 regulates cell division, apoptosis and cell migration.Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K., Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E., Blagden S.P.Nucleic Acids Res. 38:5542-5553(2010) Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1.Aoyagi M., Gaspar M., Shenk T.E.Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) A stimulatory role for the La-related protein 4B in translation.Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.RNA 16:1488-1499(2010) 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) Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination.Skourti-Stathaki K., Proudfoot N.J., Gromak N.Mol. Cell 42:794-805(2011) Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation.Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P., Roux P.P.Genes Dev. 28:357-371(2014) Recognition of polyadenylate RNA by the poly(A) -binding protein.Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.Cell 98:835-845(1999) Structure and function of the C-terminal PABC domain of human poly(A) -binding protein.Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001) Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with chemical exchange using two overlapping motifs.Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I., Shimada I.Submitted (MAY-2009) to the PDB data bankMolecular determinants of PAM2 recognition by the MLLE domain of poly(A) -binding protein.Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.J. Mol. Biol. 397:397-407(2010) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 46367787
• NCBI GeneID: 26986
• NCBI Accession #: NP_002559.2
• NCBI GenBank Nucleotide #: NM_002568.3
• UniProt Accession #: P11940; Q15097; Q93004
• Molecular Weight: 57.8 kDa
• NCBI Official Full Name: polyadenylate-binding protein 1
• NCBI Official Synonym Full Names: poly(A) binding protein, cytoplasmic 1
• NCBI Official Symbol: PABPC1
• NCBI Official Synonym Symbols: PAB1; PABP; PABP1; PABPC2; PABPL1
• NCBI Protein Information: polyadenylate-binding protein 1
• UniProt Protein Name: Polyadenylate-binding protein 1
• Protein Family: Polyadenylate-binding protein
• UniProt Gene Name: PABPC1
• UniProt Synonym Gene Names: PAB1; PABP1; PABPC2; PABP-1; Poly(A)-binding protein 1
• UniProt Entry Name: PABP1_HUMAN

NCBI Description

This gene encodes a poly(A) binding protein. The protein shuttles between the nucleus and cytoplasm and binds to the 3' poly(A) tail of eukaryotic messenger RNAs via RNA-recognition motifs. The binding of this protein to poly(A) promotes ribosome recruitment and translation initiation; it is also required for poly(A) shortening which is the first step in mRNA decay. The gene is part of a small gene family including three protein-coding genes and several pseudogenes.[provided by RefSeq, Aug 2010]

Uniprot Description

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299). Positively regulates the replication of dengue virus (DENV) (PubMed:26735137).