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Recombinant human RNA polymerase II CTD repeat YSPTSPS protein is a Human Fragment protein, in the 1586 to 1951 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
Alternative names=DNA-directed RNA polymerase II subunit RPB1, RNA polymerase II subunit B1, DNA-directed RNA polymerase II subunit A, DNA-directed RNA polymerase III largest subunit, RNA-directed RNA polymerase II subunit RPB1, POLR2, POLR2A
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
Yes
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Recombinant human RNA polymerase II CTD repeat YSPTSPS protein is a Human Fragment protein, in the 1586 to 1951 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
Alternative names=DNA-directed RNA polymerase II subunit RPB1, RNA polymerase II subunit B1, DNA-directed RNA polymerase II subunit A, DNA-directed RNA polymerase III largest subunit, RNA-directed RNA polymerase II subunit RPB1, POLR2, POLR2A
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
Yes
1 unit equals 1 nanogram of purified protein. 20 units are sufficient for reconstituted transcription assay and 100 units are sufficient for a protein-protein interaction assay. Has been applied in in vitro transcription assays, splicing assays and protein-protein interactions assays.
42.2 kDa
1586 to 1951
Fragment
No
Recombinant
Human
pH: 7.9
Constituents: 20% Glycerol (glycerin, glycerine), 0.75% Potassium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00584% EDTA
Liquid
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative 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-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD (PubMed:24207025). Methylation and dimethylation have a repressive effect on target genes expression (By similarity).
Belongs to the RNA polymerase beta' chain family.
The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated (PubMed:28076779). The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.
Nucleus
Dry Ice
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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