• Call +1.858.633.0165 or Fax +1.858.633.0166 or Contact Us

Polyadenylate-Binding Protein 1 (PABPC1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS960232

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… More details

$275 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
PDF
Sample Manual Insert View PDF
PDF
Testing Data View PDF
PDF
Certificate of Analysis (COA) View PDF
PDF
QC Report View PDF
PDF
Material Safety Data Sheet View PDF
PDF
Technical Datasheet View PDF
PDF
Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Polyadenylate-binding protein 1 (PABPC1), Recombinant Protein
Full Product Name
Recombinant Human Polyadenylate-binding protein 1
Sequence
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT KPLYVALAQR
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
57.8 kDa
Sequence Positions
1-370aa; Partial
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
604679
3D Structure
ModBase 3D Structure for P11940
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 support@mybiosource.com for more details.
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for PABPC1 recombinant protein

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.

Other Notes

Small volumes of PABPC1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for PABPC1 purchase

MBS960232 is a recombinant protein targeting PABPC1. Also known as Recombinant Human Polyadenylate-binding protein 1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for PABPC1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Polyadenylate-binding protein 1
UniProt Gene Name
PABPC1
UniProt Synonym Gene Names
PAB1; PABP1; PABPC2; PABP-1; Poly(A)-binding protein 1
UniProt Entry Name
PABP1_HUMAN
NCBI Protein Information
polyadenylate-binding protein 1

NCBI Summary for PABPC1

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]
Show more

UniProt Comments for PABPC1

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).
Show more

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

Request a Quote

Please fill out the form below and our representative will get back to you shortly.

MBS000000
Contact Us

Please fill out the form below and our representative will get back to you shortly.

MBS000000