SRP2120
RNA Polymerase II, C-terminal domain, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
Synonyme(s) :
POLRA, RPB1, RPO2, RPOL2, hRPB220
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.26
Produits recommandés
Source biologique
human
Produit recombinant
expressed in E. coli
Pureté
≥70% (SDS-PAGE)
Forme
frozen liquid
Poids mol.
~68.1 kDa
Conditionnement
pkg of 10 μg
Conditions de stockage
avoid repeated freeze/thaw cycles
Couleur
clear colorless
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... POLR2A(5430)
Catégories apparentées
Actions biochimiques/physiologiques
The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA pol II in vivo: IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongation complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFb, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identified. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing.
The CTD works as a binding scaffold for nuclear factors through its phosphorylation. It is suggested to be also involved in chromatin structure modification, DNA damage/repair, protein degradation and synthesis, RNA degradation, snRNA (small nuclear RNA) modification, and snoRNP (small nucleolar ribonucleoprotein) biogenesis.
Forme physique
Clear and colorless frozen liquid solution
Notes préparatoires
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
RNA polymerase II C-terminal domain required for enhancer-driven transcription.
Gerber HP, et al.
Nature, 374, 660-662 (1995)
Phosphorylation and functions of the RNA polymerase II CTD.
Phatnani HP and Greenleaf AL
Genes & Development, 20, 2922-2936 (2006)
T O'Brien et al.
Nature, 370(6484), 75-77 (1994-07-07)
The carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II is essential in vivo, and is found in either an unphosphorylated (IIa) or hyperphosphorylated (IIo) form. The Drosophila uninduced hsp70 and hsp26 genes, and the constitutively expressed beta-1
H Lu et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(22), 10004-10008 (1991-11-15)
The two forms of RNA polymerase II that exist in vivo, phosphorylated (IIO) and nonphosphorylated (IIA), were purified to apparent homogeneity from HeLa cells. The nonphosphorylated form preferentially binds to the preinitiation complex. RNA polymerase II in the complex was
The role of multisite phosphorylation in the regulation of RNA polymerase II activity.
M E Dahmus
Progress in nucleic acid research and molecular biology, 48, 143-179 (1994-01-01)
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique