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Monoclonal Antibodies

Anti-PCNA [5E6/2]

Invented at Cancer Research UK London Research Institute: Clare Hall Laboratories
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Adapted from Parker et al. 2008. EMBO J; 27(18):2422-31. PMID: 18701921. Figure. Lethal amounts of DNA damage cause PCNA hyper-sumoylation in WT, but not in pol30-52 cells. Cultures were arrested in G1, S or G2 phase or left asynchronous (AS) and treated were indicated with 0.3% methyl methanesulphonate (MMS) for 90 min. In the right-hand panel, both the WT and the pol30-52 strain (52) were treated during exponential growth. Total cell extracts prepared under denaturing conditions were analysed by western blotting using PCNA-specific antibody. The asterisk indicates a cross-reacting band visible with some batches of the antibody.
Adapted from Davies et al. 2008. Mol Cell; 29(5):625-36. PMID: 18342608. Figure. (A) Cell-cycle dependence of PCNA modification. Cells arrested in G1, S, and G2 phase were treated with 0.02% MMS for 90 min where indicated, and modifications of HisPCNA, isolated under denaturing conditions, were detected by western blot. (B) Effects of RAD18 overexpression on PCNA modification throughout the cell cycle. Cells were treated and analyzed as in (A). Note that, in this panel, monoubiquitylated PCNA is abundant enough to be detected by the anti-ubiquitin antibody, which recognizes this form very poorly (Hoege et al., 2002). Rad18 was detected in total cell extracts.
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Catalogue Number 151456
Applications ELISA IP WB
Antigen/Gene or Protein Targets Proliferating cell nuclear antigen, (PCNA), also known as cyclin or polymerase delta accessory protein.
Reactivity Saccharomyces cerevisiae
Relevance Monoclonal antibody which binds PCNA, a tumour proliferation marker.

Background and Research Application
PCNA, also known as polymerase delta auxiliary protein, is essential for DNA replication and is involved in DNA excision and mismatch repair pathways. It is required for cellular DNA synthesis, and in vitro replication of SV40 DNA. It helps to co-ordinate the leading and lagging strand synthesis at the replication fork. PCNA binds to the CDK inhibitor p21, the structure-specific endonucleases Fen1 and XPG, and DNA cytosine 5-methyltransferase (MCMT). PCNA is the replicative clamp protein, an essential processivity factor for DNA polymerases and an interaction partner for many other proteins. This protein is potentially a therapeutic target in cancer therapy and a useful marker for identifying the proliferation status of tumour tissue (i.e. relevant to prognosis).
This antibody recognises endogenous PCNA protein from budding yeast, Sacchoromyces cerevisiae.
Host Mouse
Immunogen Purified recombinant His6-POL30 (PCNA) from budding yest, Saccharomyces cerevisiae, produced in Escherichia coli
Immunogen UniProt ID P12004
Positive Control Wild type budding yeast expressing native POL30 (PCNA)
Subclass IgG1
Molecular Weight (kDa) 30
Myeloma Used Sp2/0-Ag14
Recommended Growing Conditions RPMI + 5% FCS
Strain CD1
Notes Production Details
Purified using multi-step affinity chromatography with protein A.

Storage Conditions
Store at -20 degrees frozen. Avoid repeated freeze/thaw cycles.

Concentration
1mg/ml as standard
Research Area Cancer, Cell Cycle, Cell Type or Organelle Marker, Epigenetics & Nuclear Signalling

References

There are 10 reference entries for this reagent.

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References: 10 entries

Paul Solomon Devakumar et al. 2019. Nucleic Acids Res. 47(13):6826-6841. PMID: 31114918.

WB

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Schalbetter et al. 2015. Proc Natl Acad Sci U S A. 112(33):E4565-70. PMID: 26240319.

View  

Kubota et al. 2011. Mol Cell Proteomics. 10(7):M110.005561. PMID: 21505101.

View  

Quantitative proteomic analysis of chromatin reveals that Ctf18 acts in the DNA replication checkpoint.

Europe PMC ID: 21505101

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Parker et al. 2008. EMBO J. 27(18):2422-31. PMID: 18701921.

WB

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SUMO modification of PCNA is controlled by DNA.

Europe PMC ID: 18701921

View  

Davies et al. 2008. Mol Cell. 29(5):625-36. PMID: 18342608.

View  

Activation of ubiquitin-dependent DNA damage bypass is mediated by replication protein a.

Europe PMC ID: 18342608

View  

Windecker et al. 2008. J Mol Biol. 376(1):221-31. PMID: 18155241.

WB

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Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae.

Europe PMC ID: 18155241

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References: 10 entries

Paul Solomon Devakumar et al. 2019. Nucleic Acids Res. 47(13):6826-6841. PMID: 31114918.

WB

View  

Schalbetter et al. 2015. Proc Natl Acad Sci U S A. 112(33):E4565-70. PMID: 26240319.

View  

Kubota et al. 2011. Mol Cell Proteomics. 10(7):M110.005561. PMID: 21505101.

View  

Quantitative proteomic analysis of chromatin reveals that Ctf18 acts in the DNA replication checkpoint.

View  

Parker et al. 2008. EMBO J. 27(18):2422-31. PMID: 18701921.

WB

View  

SUMO modification of PCNA is controlled by DNA.

View  

Davies et al. 2008. Mol Cell. 29(5):625-36. PMID: 18342608.

View  

Activation of ubiquitin-dependent DNA damage bypass is mediated by replication protein a.

View  

Windecker et al. 2008. J Mol Biol. 376(1):221-31. PMID: 18155241.

WB

View  

Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae.

View  

Add a reference

Inventor Information