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TGS1 recombinant protein :: Trimethylguanosine synthase Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS1460726
SDS-Page
Unit / Price
0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.05 mg (Yeast)  /  $700 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
0.05 mg (Baculovirus)  /  $850 +1 FREE 8GB USB
0.2 mg (Yeast)  /  $945 +1 FREE 8GB USB
0.5 mg (Yeast)  /  $1,060 +1 FREE 8GB USB
0.1 mg (Baculovirus)  /  $1,075 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,090 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
0.5 mg (Baculovirus)  /  $1,555 +1 FREE 8GB USB
1 mg (Yeast)  /  $1,610 +2 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $1,665 +2 FREE 8GB USB
1 mg (Baculovirus)  /  $2,080 +2 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Trimethylguanosine synthase (TGS1), Recombinant Protein

★Popular Item★
 Also Known As   

Recombinant Human Trimethylguanosine synthase

 Product Synonym Names    CLL-associated antigen KW-2; Cap-specific guanine-N2 methyltransferase; Hepatocellular carcinoma-associated antigen 137; Nuclear receptor coactivator 6-interacting protein; PRIP-interacting protein with methyltransferase motif; PIMT; PIPMT
 Product Gene Name   

TGS1 recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 MBS1460726 COA    COA PDF
 Sequence Positions    713-853aa; Partial
 Sequence    MRVIAIDIDP VKIALARNNA EVYGIADKIE FICGDFLLLA SFLKADVVFL SPPWGGPDYA TAETFDIRTM MSPDGFEIFR LSKKITNNIV YFLPRNADID QVASLAGPGG QVEIEQNFLN NKLKTITAYF GDLIRRPASE T
 OMIM    606461
 3D Structure    ModBase 3D Structure for Q96RS0
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 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.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of TGS1 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.
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Related Product Information for TGS1 recombinant protein

   Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m7G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation.
 Product Categories/Family for TGS1 recombinant protein    Epigenetics and Nuclear Signaling
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 SDS-Page of TGS1 recombinant protein    TGS1 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for TGS1. It may not necessarily be applicable to this product.
 NCBI GI #    151301096
 NCBI GeneID    96764
 NCBI Accession #    NP_079107.6 [Other Products]
 NCBI GenBank Nucleotide #    NM_024831.7 [Other Products]
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 UniProt Primary Accession #    Q96RS0 [Other Products]
 UniProt Secondary Accession #    Q5GH23; Q8TDG9; Q96QU3; Q9H5V3; A6NJQ5 [Other Products]
 UniProt Related Accession #    Q96RS0 [Other Products]
 Molecular Weight    31.64kD
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 NCBI Official Full Name    trimethylguanosine synthase isoform 1
 NCBI Official Synonym Full Names    trimethylguanosine synthase 1
 NCBI Official Symbol    TGS1 [Similar Products]
 NCBI Official Synonym Symbols   
PIMT; PIPMT; NCOA6IP
[Similar Products]
 NCBI Protein Information    trimethylguanosine synthase
 UniProt Protein Name    Trimethylguanosine synthase
 UniProt Synonym Protein Names   
CLL-associated antigen KW-2; Cap-specific guanine-N2 methyltransferase; Hepatocellular carcinoma-associated antigen 137; Nuclear receptor coactivator 6-interacting protein; PRIP-interacting protein with methyltransferase motif; PIMT; PIPMT
 Protein Family    Trimethylguanosine synthase
 UniProt Gene Name    TGS1 [Similar Products]
 UniProt Synonym Gene Names    HCA137; NCOA6IP; PIMT; PIMT; PIPMT [Similar Products]
 UniProt Entry Name    TGS1_HUMAN
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 UniProt Comments for TGS1    PIMT: a nuclear protein and apparent methyltransferase. Binds S-adenosyl-L-methionine and RNA. Plays a role in transcriptional regulation. Interacts with NCOA, CBP, p300, and PPARBP. Ubiquitously expressed. High expression in heart, skeletal muscle, kidney, liver and placenta.

Protein type: RNA processing; Nuclear receptor co-regulator; EC 2.1.1.-; Methyltransferase

Chromosomal Location of Human Ortholog: 8q11

Cellular Component: Cajal body; cytoplasm; cytosol; extracellular space; nucleolus; nucleoplasm; nucleus; small nuclear ribonucleoprotein complex

Molecular Function: protein binding

Biological Process: cellular lipid metabolic process; gene expression; regulation of transcription, DNA-dependent; ribonucleoprotein complex biogenesis and assembly; RNA capping; spliceosomal snRNP biogenesis; transcription, DNA-dependent
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Product References and Citations for TGS1 recombinant protein

   Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function.Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001) Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX.Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.Blood 100:2123-2131(2002) Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies.Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.J. Immunol. 169:1102-1109(2002) 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) SEREX-defined rhabdomyosarcoma antigens.Behrends U., Gotz C., Mautner J. 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) Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments.Verheggen C., Lafontaine D.L.J., Samarsky D., Mouaikel J., Blanchard J.-M., Bordonne R., Bertrand E.EMBO J. 21:2736-2745(2002) Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation.Misra P., Qi C., Yu S., Shah S.H., Cao W.Q., Rao M.S., Thimmapaya B., Zhu Y., Reddy J.K.J. Biol. Chem. 277:20011-20019(2002) Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localize to the cytoplasm and nucleus.Enuenlue I., Papai G., Cserpan I., Udvardy A., Jeang K.-T., Boros I.Biochem. Biophys. Res. Commun. 309:44-51(2003) Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron.Mouaikel J., Narayanan U., Verheggen C., Matera A.G., Bertrand E., Tazi J., Bordonne R.EMBO Rep. 4:616-622(2003) Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies.Lemm I., Girard C., Kuhn A.N., Watkins N.J., Schneider M., Bordonne R., Luehrmann R.Mol. Biol. Cell 17:3221-3231(2006) Genetic and biochemical analysis of yeast and human cap trimethylguanosine synthase functional overlap of 2,2,7-trimethylguanosine caps, small nuclear ribonucleoprotein components, pre-mRNA splicing factors, and RNA decay pathways.Hausmann S., Zheng S., Costanzo M., Brost R.L., Garcin D., Boone C., Shuman S., Schwer B.J. Biol. Chem. 283:31706-31718(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) 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) 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) Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1.Monecke T., Dickmanns A., Strasser A., Ficner R.Acta Crystallogr. D 65:332-338(2009) Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1.Monecke T., Dickmanns A., Ficner R.Nucleic Acids Res. 37:3865-3877(2009)
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 Research Articles on TGS1    1. PIMT was identified as a key player responsible for glycated low density lipoproteins induced vascular endothelial cell apoptosis.
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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.
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Products associated with TGS1 recombinant proteinPathways associated with TGS1 recombinant protein
 Reference Product  PubMed Publications
 SNUPN recombinant protein  >1 publications with TGS1 and SNUPN
 NCOA6 recombinant protein  >1 publications with TGS1 and NCOA6
 Products by Pathway  Pathway Diagram
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 BMAL1:CLOCK,NPAS2 Activates Circadian Gene Expression Pathway antibodies  BMAL1:CLOCK,NPAS2 Activates Circadian Gene Expression Pathway Diagram
 Circadian Clock Pathway antibodies  Circadian Clock Pathway Diagram
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 Fatty Acid, Triacylglycerol, And Ketone Body Metabolism Pathway antibodies  Fatty Acid, Triacylglycerol, And Ketone Body Metabolism Pathway Diagram
 Gene Expression Pathway antibodies  Gene Expression Pathway Diagram
 Generic Transcription Pathway antibodies  Generic Transcription Pathway Diagram
 Metabolism Pathway antibodies  Metabolism Pathway Diagram
 Metabolism Of Lipids And Lipoproteins Pathway antibodies  Metabolism Of Lipids And Lipoproteins Pathway Diagram
 Metabolism Of Non-coding RNA Pathway antibodies  Metabolism Of Non-coding RNA Pathway Diagram
Diseases associated with TGS1 recombinant proteinOrgans/Tissues associated with TGS1 recombinant protein
 Disease Name  Pubmed Publications
 Atrophy Antibodies  >1 publications with TGS1 and Atrophy
 Organ/Tissue Name  Pubmed Publications
 Uterus Antibodies  >1 publications with TGS1 and Uterus
 Testis Antibodies  >1 publications with TGS1 and Testis
 Blood Antibodies  >1 publications with TGS1 and Blood
 Muscle Antibodies  >1 publications with TGS1 and Muscle
 Brain Antibodies  >1 publications with TGS1 and Brain
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