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Anti-Phospho-POLR2A (S5) antibody

SKU Product Brand Unit Availability Price Quantity  
AB-06-3537
Anti-Phospho-POLR2A (S5) antibody
Erpan Tech In stock

Specifications        

Product Cat#: AB-06-3537
Product type: Primary antibody
Antigen: Phospho-POLR2A (S5)
Immunogen: Synthetic phospho-peptide corresponding to residues surrounding Ser5 of human POLR2A.
Species immunized: Rabbit
Isotype: IgG
Applications: Western Blot (1:400-1:1000); Immunohistochemistry (1:40-1:200); Immunocytochemistry (1:90-1:500); Flow Cytometry (1:40-1:100); Immunoprecipitation; Immunofluorescence
Reactivity: Human, Mouse, Rat
Clonality (clone number): Monoclonal (JM51-21)
Form: Liquid
Buffer: Tris-HCl buffer (pH7.4), 1% BSA; 40% glycerol, 0.05% NaN3.
Concentration: 1 mg/ml
Purity: Protein A affinity purified
Storage: Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles.
Alternative names: DNA directed RNA polymerase II A antibody
DNA-directed RNA polymerase II largest subunit RNA polymerase II 220 kd subunit antibody
DNA-directed RNA polymerase II subunit A antibody
DNA-directed RNA polymerase II subunit RPB1 antibody
DNA-directed RNA polymerase III largest subunit antibody
HRPB220 antibody
HsRPB1 antibody
POLR2 antibody
Polr2a antibody
POLRA antibody
Polymerase (RNA) II (DNA directed) polypeptide A 220kDa antibody
Polymerase (RNA) II (DNA directed) polypeptide A antibody
RNA polymerase II subunit B1 antibody
RNA-directed RNA polymerase II subunit RPB1 antibody
RPB1 antibody
RPB1_HUMAN antibody
RPBh1 antibody
RpIILS antibody
RPO2 antibody
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Target information

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 . Methylation and dimethylation have a repressive effect on target genes expression (By similarity).By similarity5 Publications
(Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.

Miscellaneous

The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.

Provider

Erpantech Laboratory

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