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Nuclear Pore Complex Protein Nup153 (NUP153) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS949865

Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs.… More details

$500 / 0.02 mg (Yeast) +1 FREE 8GB USB
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Nuclear pore complex protein Nup153, Recombinant Protein
Full Product Name
Recombinant Human Nuclear pore complex protein Nup153
Product Synonym Names
153 kDa nucleoporin; Nucleoporin Nup153
Sequence
KAGSSWQCDT CLLQNKVTDN KCIACQAAKL SPRDTAKQTG IETPNKSGKT TLSASGTGFG DKFKPVIGTW DCDTCLVQNK PEAIKCVACE TPKPGTCVKR ALTLTVVSES AETMTASSSS CTVTTGTLGF GDKFKRPIGS WECSVCCVSN NAEDNKCVSC MSEKPGSSVP ASSSSTVPVS LPSGGSLGLE KFKKPEGSWD CELCLVQNKA DSTKCLACES AKPG
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
27.3 kDa
Sequence Positions
657-880aa; 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
603948
3D Structure
ModBase 3D Structure for P49790

Product Categories/Family for NUP153 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for NUP153 recombinant protein

Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.McMorrow I., Bastos R., Horton H., Burke B.Biochim. Biophys. Acta 1217:219-223(1994) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method.Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O. The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Bienvenut W.V., Dozynkiewicz M., Norman J.C.Submitted (MAR-2009) to UniProtKB Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.Brownawell A.M., Macara I.G.J. Cell Biol. 156:53-64(2002) Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.Frosst P., Guan T., Subauste C., Hahn K., Gerace L.J. Cell Biol. 156:617-630(2002) Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.Hase M.E., Cordes V.C.Mol. Biol. Cell 14:1923-1940(2003) Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.Mol. Biol. Cell 15:4261-4277(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 probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(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) Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1.Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.J. Virol. 83:6522-6533(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) 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) Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.EMBO J. 29:1659-1673(2010) Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.Nakano H., Funasaka T., Hashizume C., Wong R.W.J. Biol. Chem. 285:10841-10849(2010) Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket.Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., Stoeber M., Pante N., Kann M.PLoS Pathog. 6:E1000741-E1000741(2010) Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.Sci. Signal. 3:RA2-RA2(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) 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) Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage.Kose S., Furuta M., Imamoto N.Cell 149:578-589(2012) Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.Rajanala K., Nandicoori V.K.PLoS ONE 7:E29921-E29921(2012) 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) Solution structure of the second and third ZF-RANBP domains from human nuclear pore complex protein NUP153.RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bankSolution structure of the second ZF-ranbp domain from human nuclear pore complex protein nup153.RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank+Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of NUP153 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 NUP153 purchase

MBS949865 is a recombinant protein targeting NUP153. Also known as Recombinant Human Nuclear pore complex protein Nup153. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for NUP153. 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
nuclear pore complex protein Nup153 isoform 1
NCBI Official Synonym Full Names
nucleoporin 153kDa
NCBI Official Symbol
NUP153
NCBI Official Synonym Symbols
N153; HNUP153
UniProt Protein Name
Nuclear pore complex protein Nup153
UniProt Synonym Protein Names
153 kDa nucleoporin; Nucleoporin Nup153
UniProt Gene Name
NUP153
UniProt Entry Name
NU153_HUMAN
NCBI Protein Information
nuclear pore complex protein Nup153

NCBI Summary for NUP153

Nuclear pore complexes regulate the transport of macromolecules between the nucleus and cytoplasm. They are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are glycoproteins found in nuclear pores and contain characteristic pentapeptide XFXFG repeats as well as O-linked N-acetylglucosamine residues oriented towards the cytoplasm. The protein encoded by this gene has three distinct domains: a N-terminal region containing a pore targeting and an RNA-binding domain domain, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, May 2013]
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UniProt Comments for NUP153

NUP153: Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane.

Protein type: Nuclear export; Nucleoporin

Chromosomal Location of Human Ortholog: 6p22.3

Cellular Component: annulate lamellae; cytoplasm; nuclear inclusion body; nuclear membrane; nuclear pore; nucleolus; nucleoplasm

Molecular Function: chromatin binding; double-stranded DNA binding; identical protein binding; nuclear localization sequence binding; nucleocytoplasmic transporter activity; protein anchor; protein binding; Ran GTPase binding; structural constituent of nuclear pore; zinc ion binding

Biological Process: carbohydrate metabolic process; cellular protein metabolic process; cytokine and chemokine mediated signaling pathway; entry of virus into host cell; gene expression; glucose transport; hexose transport; mitosis; mitotic cell cycle; mitotic nuclear envelope disassembly; modification by virus of host cellular process; mRNA transport; negative regulation of RNA export from nucleus; nuclear pore complex assembly; post-translational protein modification; protein sumoylation; protein transport; RNA-mediated gene silencing; transmembrane transport; tRNA processing; viral infectious cycle; viral reproduction; viral transcription; virus-host interaction
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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.

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