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Transcription Initiation Factor IIB (GTF2B) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS969533

General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. More details

$385 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Transcription initiation factor IIB (GTF2B), Recombinant Protein
Full Product Name
Recombinant Human Transcription initiation factor IIB
Product Gene Name
Product Synonym Names
General transcription factor TFII; BS300-II
Sequence
MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE ITTMADRINL PRNIVDRTNN LFKQVYEQKS LKGRANDAIA SACLYIACRQ EGVPRTFKEI CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF PTDFKFDTPV DKLPQL
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
50.8 kDa
Sequence Positions
1-316aa; Full Length
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
189963
3D Structure
ModBase 3D Structure for Q00403

Product Categories/Family for GTF2B recombinant protein

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

Product References and Citations for GTF2B recombinant protein

Cloning of a human gene encoding the general transcription initiation factor IIB.Ha I., Lane W.S., Reinberg D.Nature 352:689-695(1991) Sequence of general transcription factor TFIIB and relationships to other initiation factors.Malik S., Hisatake K., Sumimoto H., Horikoshi M., Roeder R.G.Proc. Natl. Acad. Sci. U.S.A. 88:9553-9557(1991) 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) Human protein factory for converting the transcriptome into an in vitro-expressed proteome.Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.Nat. Methods 5:1011-1017(2008) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II) .Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.J. Biol. Chem. 267:17617-17623(1992) ICP4, the major transcriptional regulatory protein of herpes simplex virus type 1, forms a tripartite complex with TATA-binding protein and TFIIB.Smith C.A., Bates P., Rivera-Gonzalez R., Gu B., DeLuca N.A.J. Virol. 67:4676-4687(1993) Isolation and characterization of a cDNA encoding a new type of human transcription elongation factor S-II.Umehara T., Kida S., Yamamoto T., Horikoshi M.Gene 167:297-302(1995) The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein.Tong X., Wang F., Thut C.J., Kieff E.J. Virol. 69:585-588(1995) The human immunodeficiency virus type 1 Vpr transactivator cooperation with promoter-bound activator domains and binding to TFIIB.Agostini I., Navarro J.-M., Rey F., Bouhamdan M., Spire B., Vigne R., Sire J.J. Mol. Biol. 261:599-606(1996) The HIV-1 Vpr co-activator induces a conformational change in TFIIB.Agostini I., Navarro J.M., Bouhamdan M., Willetts K., Rey F., Spire B., Vigne R., Pomerantz R., Sire J.FEBS Lett. 450:235-239(1999) 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) 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) 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) Solution structure of the C-terminal core domain of human TFIIB similarity to cyclin A and interaction with TATA-binding protein.Bagby S., Kim S., Maldonado E., Tong K.I., Reinberg D., Ikura M.Cell 82:857-867(1995) Crystal structure of a TFIIB-TBP-TATA-element ternary complex.Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K., Roeder R.G., Burley S.K.Nature 377:119-128(1995) Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription.Chen H.T., Legault P., Glushka J., Omichinski J.G., Scott R.A.Protein Sci. 9:1743-1752(2000) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of GTF2B 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 GTF2B purchase

MBS969533 is a recombinant protein targeting GTF2B. Also known as Recombinant Human Transcription initiation factor IIB. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for GTF2B. 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
transcription initiation factor IIB
NCBI Official Synonym Full Names
general transcription factor IIB
NCBI Official Symbol
GTF2B
NCBI Official Synonym Symbols
TF2B; TFIIB
UniProt Protein Name
Transcription initiation factor IIB
UniProt Synonym Protein Names
General transcription factor TFIIB; S300-II
UniProt Gene Name
GTF2B
UniProt Synonym Gene Names
TF2B; TFIIB
UniProt Entry Name
TF2B_HUMAN
NCBI Protein Information
transcription initiation factor IIB

NCBI Summary for GTF2B

This gene encodes the general transcription factor IIB, one of the ubiquitous factors required for transcription initiation by RNA polymerase II. The protein localizes to the nucleus where it forms a complex (the DAB complex) with transcription factors IID and IIA. Transcription factor IIB serves as a bridge between IID, the factor which initially recognizes the promoter sequence, and RNA polymerase II. [provided by RefSeq, Jul 2008]
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UniProt Comments for GTF2B

GTF2B: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. Associates with TFIID-IIA (DA complex) to form TFIID-IIA- IIB (DAB-complex) which is then recognized by polymerase II. Interacts with the transcription elongation factor TCEA2. Interacts with HIV-1 Vpr. Interacts with GPBP1. Interacts with Epstein-Barr virus EBNA2. Belongs to the TFIIB family.

Protein type: Transcription factor; Acetyltransferase; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 1p22-p21

Cellular Component: nucleolus; nucleoplasm; nucleus

Molecular Function: protein binding; thyroid hormone receptor binding; transcription factor binding; zinc ion binding

Biological Process: gene expression; regulation of transcription, DNA-dependent; RNA elongation from RNA polymerase II promoter; transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase II promoter; viral reproduction
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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.

Product PubMed Publications

Diseases associated with GTF2B recombinant protein

Organs/Tissues associated with GTF2B recombinant protein

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