Open reading frame 14 (ORF14) of Varicella zoster encodes for late glycoprotein C (gC). VZV gC is 105-kDa highly glycosylated protein with almost one third of its molecular weight consisting of oligosaccharide chains on four predicted N-linked glycosylation sites and 25 O-linked mucin type sites (Journal of Virology (1990) 64, 4540-8, Virology (2008) 382, 171-81). Unlike other major glycoproteins in herpesviruses, it shares only 30% homology with HSV-1 gC (Reviews of infectious diseases (1991) 13, pp. S960–S963). It shows delayed transcription and protein expression when compared with other major VZV glycoproteins (gE, gI, gH and gB) as well compared with HSV gC in infected cells (Virology (2008) 382, 171-81, Current Topics in Microbiology and Immunology (2010) 342, 113-28. VZV gC expression is reduced in VZV-infected neurons on both transcriptional and protein level (Journal of Virology (2013) 87, 9643–9648 6). Our anti VZV ORF14 antibody VZ 14.12 shows that the VZV gC is located predominantly in the Golgi. Our anti-VZV ORF14 antibody VZ 14.12 works in ELISA (on immunogen), IF (on VZV infected cells) and each LOT is validated for Western blot (of VZV infected cell lysates, described in J Virol. 2013 Jun;87(12):6943-54.).
Clone: VZ 14.12
Catalog No.: HR-VZV-09
Host Species: Mouse
Reactivity: Varicella zoster virus
Antigen/Immunogen: The immunogen consisted of full length ORF14 and was produced in E.coli
Tested Applications: ELISA; IF; WB
Recommended Dilution: n/a
Varicella zoster virus
The immunogen consisted of full length ORF14 and was produced in E.coli
ELISA; IF; WB
€200.00 – €700.00
|STORAGE||Long term -20 °C, short term +4 °C. Avoid freeze-thaw cycles.|
|LIGHT CHAIN TYPE||kappa|
|REFERENCES||Lenac et al., J Virol, 2013|
VZV ORF4 encodes an IE4 protein that acts as transactivator of several immediate early, early and late VZV genes. Dimerization of IE4 is required for its transactivation function.
ORF31 is one of five glycoprotein ORFs in VZV genome. It encodes for gB, a type I membrane protein containing 868 aa which in mature form exists as a highly glycosylated disulfide-linked heterodimer (Annu Rev Microbiol 1990. 44: 59-80).