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Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase, Recombinant

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產(chǎn)品名稱: Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase, Recombinant
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Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase, Recombinant Protein


Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase, Recombinant  的詳細介紹
Product Name

Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase (FTSJ1), Recombinant Protein

Full Product Name

Recombinant Human Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase

Product Synonym Names
2'-O-ribose RNA methyltransferase TRM7 homolog
Product Gene Name

FTSJ1 recombinant protein

[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
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Sequence Positions
1-329aa; Full Length
Sequence
MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD LSSYDSDRSY PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV DTFPQPLAAP QCHTLLAPEM EDNEMSCSP
OMIM
300499
3D Structure
ModBase 3D Structure for Q9UET6
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 13485:2003 and EN ISO 13485:2012 Certified Laboratory.
Other Notes
Small volumes of FTSJ1 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
FTSJ1 recombinant protein
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Product Categories/Family for FTSJ1 recombinant protein
Epigenetics and Nuclear Signaling

SDS-PAGE of FTSJ1 recombinant protein
FTSJ1 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 FTSJ1. It may not necessarily be applicable to this product.
NCBI GI #
531990794
NCBI GeneID
24140
NCBI Accession #
NP_001269086.1 [Other Products]
NCBI GenBank Nucleotide #
NM_001282157.1 [Other Products]
UniProt Primary Accession #
Q9UET6 [Other Products]
UniProt Secondary Accession #
O75670; B2RCJ0[Other Products]
UniProt Related Accession #
Q9UET6[Other Products]
Molecular Weight
40.2kD
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NCBI Official Full Name
putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase isoform c
NCBI Official Synonym Full Names
FtsJ RNA methyltransferase homolog 1 (E. coli)
NCBI Official Symbol
FTSJ1??[Similar Products]
NCBI Official Synonym Symbols
JM23; MRX9; SPB1; CDLIV; MRX44; TRMT7
??[Similar Products]
NCBI Protein Information
putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase
UniProt Protein Name
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase
UniProt Synonym Protein Names
2'-O-ribose RNA methyltransferase TRM7 homolog
UniProt Gene Name
FTSJ1??[Similar Products]
UniProt Entry Name
TRM7_HUMAN
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NCBI Summary for FTSJ1
This gene encodes a member of the methyltransferase superfamily. The encoded protein localizes to the nucleolus, binds to S-adenosylmethionine, and may be involved in the processing and modification of ribosomal RNA. Mutations in this gene are associated with mental retardation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]
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UniProt Comments for FTSJ1
FTSJ1: Defects in FTSJ1 are the cause of mental retardation X- linked type 44 (MRX44). Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. Belongs to the methyltransferase superfamily. RlmE family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.1.1.205; Methyltransferase

Chromosomal Location of Human Ortholog: Xp11.23

Cellular Component: cytoplasm

Molecular Function: tRNA methyltransferase activity

Biological Process: tRNA methylation

Disease: Mental Retardation, X-linked 9
Product References and Citations for FTSJ1 recombinant protein
A human and yeast gene involved in cell division.Pengue G., Lutfiyya L.L., Mazzarella R.Transcription map in Xp11.23.Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A. 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) The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434:325-337(2005)

Research Articles on FTSJ1
1. These findings suggest that genetic variations in FtsJ homolog 1 (E. coli) possibly influence human cognitive ability.
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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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