Alexa Fluor 488 anti-RNA Polymerase II RPB1 Antibody anti-RNA Polymerase II RPB1 - 8WG16,BioLegend,664915

Clone 8WG16 recognizes YSPTSPS in the C-terminal domain. The antibody cross-reacts with wheat, yeast, mouse,c. elegans, x. laevis, and most eukaryotic RNAPII.Additional reported applications (for the relevant formats) include: chromatin immunoprecipitation, functional assay, and immunoprecipatation.

Host

Mouse

Reactivity

Human, Mouse

Application

ICC -Quality tested

Platform ID

BAB573504110

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Contact

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Product Specifications
Scientific Background

Specifications

NameAlexa Fluor 488 anti-RNA Polymerase II RPB1 Antibody anti-RNA Polymerase II RPB1 - 8WG16
Cat. No.664915
HostMouse
RRIDAB_2734523 (BioLegend Cat. No. 664915)AB_2734524 (BioLegend Cat. No. 664916)
IsotypeMouse IgG2a
ReactivityHuman, Mouse
ApplicationICC -Quality tested
ClonalityMonoclonal
Clone Number8WG16
Concentration0.5 mg/ml
TargetRNA Polymerase II RPB1
ImmunogenWheat germ RNA Polymerase II
PurityThe antibody was purified by affinity chromatography and conjugated with Alexa Fluor® 488 under optimal conditions.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
StorageThe antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light.Do not freeze.
Regulatory StatusResearch Use Only

Scientific Background

RPB1 is the catalytic and largest component of RNA polymerase II, which synthesizes mRNA precursors and many functional non-coding RNAs. It forms the polymerase active center together with RPB2, the second largest subunit. Polymerase II (Pol II) is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relatively to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft, and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single DNA template strand of the promoter is positioned within the central active site cleft of Pol II. Then, a bridging helix emanates from RPB1 and crosses the cleft near the catalytic site, which acts as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations during each neuocleotide addition. This promotes translocation of Pol II. Pol II moves on the template during transcription elongation. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II's largest subunit (RPB1), which serves as a platform for assembling factors that regulate transcription initiation, elongation, termination, and mRNA processing. It can act as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, being able to conform as both a replicate and transcriptase for the viral RNA circular genome.

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