SRP2013
RNA Polymerase II Peptide
≥85% (SDS-PAGE), recombinant, expressed in E. coli
Sinónimos:
POLRA, RPB1, RPO2, RPOL2, hRPB220
Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
About This Item
Código UNSPSC:
12352202
NACRES:
NA.26
Productos recomendados
Nombre del producto
RNA Polymerase II, C-terminal human, recombinant, expressed in E. coli, ≥85% (SDS-PAGE)
origen biológico
human
recombinante
expressed in E. coli
Ensayo
≥85% (SDS-PAGE)
Formulario
frozen liquid
mol peso
~42.2 kDa
envase
pkg of 10 μg
condiciones de almacenamiento
avoid repeated freeze/thaw cycles
concentración
400 μg/mL
color
clear colorless
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... POLR2A(5430)
Categorías relacionadas
Descripción general
RNA polymerase II (eukaryotic) contains around 10 subunits with a combined molecular weight of 500,000Da. The subunit structure of this enzyme is conserved amongst eukaryotes, and this subunits structure shares similarities with that of RNA pol I and III. 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.
Acciones bioquímicas o fisiológicas
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, designated 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 elongating 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.
Forma física
Clear and colorless frozen liquid solution
Nota de preparación
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Elija entre una de las versiones más recientes:
Certificados de análisis (COA)
Lot/Batch Number
¿No ve la versión correcta?
Si necesita una versión concreta, puede buscar un certificado específico por el número de lote.
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Evolution of the RNA polymerase II C-terminal domain.
Stiller JW and Hall BD
Proceedings of the National Academy of Sciences of the USA, 99(9), 6091-6096 (2002)
4 Carboxy-terminal Domain of the Largest Subunit of Eukaryotic RNA Polymerase II.
Corden JL and Ingles CJ
Cold Spring Harbor molecular case studies, 81-107 (1992)
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
RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function.
Prelich G
Eukaryotic Cell, 1(2), 153-162 (2002)
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico