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TGS1 recombinant protein :: Trimethylguanosine synthase Recombinant Protein

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Catalog # MBS1460726
Unit / Price
Scan QR to view Datasheet
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
SDS-Page
Product Name

Trimethylguanosine synthase (TGS1), Recombinant Protein

Popular Item
Full Product Name

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
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
MBS1460726 COA
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
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
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.
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.
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.

TGS1 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for TGS1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
31.64kD
NCBI Official Full Name
trimethylguanosine synthase isoform 1
NCBI Official Synonym Full Names
trimethylguanosine synthase 1
NCBI Official Symbol
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
UniProt Gene Name
UniProt Synonym Gene Names
HCA137; NCOA6IP; PIMT; PIMT; PIPMT  [Similar Products]
UniProt Entry Name
TGS1_HUMAN
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
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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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.

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Products associated withTGS1 recombinant protein
Diseases associated with TGS1 recombinant protein
 Disease Name  Pubmed Publications
 Atrophy Antibodies  >1 publications with TGS1 and Atrophy
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