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Monoclonal Antibodies

Anti-HSVUL42 [13C9]

Invented at Cancer Research UK London Research Institute: Clare Hall Laboratories
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Adapted from Iwahori S, Shirata N, Kawaguchi Y, Weller SK, Sato Y, Kudoh A, Nakayama S, Isomura H, Tsurumi T. Enhanced phosphorylation of transcription factor sp1 in response to herpes simplex virus type 1 infection is dependent on the ataxia telangiectasia-mutated protein. J Virol. 2007 Sep;81(18):9653-64. doi: 10.1128/JVI.00568-07. Epub 2007 Jul 3. PMID: 17609267; PMCID: PMC2045397. Hyperphosphorylation of Sp1 is induced even upon infection of HSV-1 mutants defective for viral PK, Us3, UL13 or UL39 gene product. HFF2 cells were infected with wild-type HSV-1 (wt HSV-1), Us3-defective virus (R7041), UL13-defective virus (R7356), or UL39-defective virus (ICP6Δ) at an MOI of 5. At 12 and 24 hpi, cells were harvested and whole-cell lysates were prepared. Equal amounts of proteins from each sample (15 μg) were subjected to immunoblot analysis with anti-Sp1, ICP4, and UL42 proteins specific antibodies.
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Catalogue Number 151033
Applications FACS IHC IF IP WB
Antigen/Gene or Protein Targets Herpes Simplex Virus protein UL42 (HSV-UL42)
Reactivity Virus
Relevance UL42 is the DNA polymerase accessory protein of herpes simplex virus type 1.
Host Mouse
Immunogen Baculovirus-expressed HSV DNA polymerase (POL) and POL/UL42 complex.
Subclass IgG1
Myeloma Used Sp2/0-Ag14
Recommended Growing Conditions DMEM + 5% FCS.
Strain Balb/c
Notes Reactivity: Herpes simplex virus (HSV)
Research Area Virology

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Iwahori et al. 2007. J Virol. 81(18):9653-64. PMID: 17609267.

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References: 1 entry

Iwahori et al. 2007. J Virol. 81(18):9653-64. PMID: 17609267.

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