FACT complex subunit SPT16 Recombinant Protein | SPT16 recombinant protein

Recombinant Arabidopsis thaliana FACT complex subunit SPT16

Cat. Num. AAA969617

• Gene Names: SPT16; global transcription factor C; SPT16; T12H20.3; T12H20_3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: FACT complex subunit SPT16; Recombinant Arabidopsis thaliana FACT complex subunit SPT16; Facilitates chromatin transcription complex subunit SPT16; SPT16 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 890-1074aa; Partial of the full length of FACT complex subunit SPT16 domain
• Sequence: DFKKDVLRVDSVPTSSLEGIKEWLDTTDIKYYESKLNLNWRQILKTITDDPQSFIDDGGWEFLNLDGSDSESGGSEESDKGYEPSDVEVESESEDEASESESLVESDDDEEEDSEQESEEEKGKTWDELEREATNADREHGVESDSEEERKRRKMKAFGKSRPGTSGGGGSSSMKNMPPSKRKHR
• Sequence Length: 1074

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for SPT16 recombinant protein

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (Probable).

Product Categories/Family for SPT16 recombinant protein

Developmental Biology

References

Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.Nature 402:769-777(1999) The Arabidopsis Information Resource (TAIR) ORF cloning and analysis of Arabidopsis transcription factor genes.Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y., Takagi M.The chromatin remodelling complex FACT associates with actively transcribed regions of the Arabidopsis genome.Duroux M., Houben A., Ruzicka K., Friml J., Grasser K.D.Plant J. 40:660-671(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 15236899
• NCBI GeneID: 826665
• NCBI Accession #: NP_192809.1
• NCBI GenBank Nucleotide #: NM_117139.2
• UniProt Accession #: O82491; C0SVH5
• Molecular Weight: 22.9kD
• NCBI Official Full Name: FACT complex subunit SPT16
• NCBI Official Symbol: SPT16
• NCBI Official Synonym Symbols: global transcription factor C; SPT16; T12H20.3; T12H20_3
• NCBI Protein Information: FACT complex subunit SPT16
• UniProt Protein Name: FACT complex subunit SPT16
• Protein Family: FACT complex
• UniProt Gene Name: SPT16
• UniProt Entry Name: SPT16_ARATH

NCBI Description

encodes a component of the FAcilitates Chromatin Transcription (FACT) complex, SPT16.Along with SSRP1 binds to the promoter of FLC.

Uniprot Description

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (Probable).