Open reading frame 5 (ORF5) of Varicella zoster encodes for envelope glycoprotein K (gK) highly conserved among alphaherpesviruses. Based on analogy to its HSV-1 homolog, VZV gK is believed to participate in membrane fusion along with other major glycoproteins. Calculated molecular mass of glycosylated form is around 40-kDa and it has two N-glycosylation sites required for the conformational integrity. VZV gK accumulates predominantly in the Golgi and it is transported to the plasma membrane of the infected cells. Afterwards, it is endocytosed from the plasma membrane and has the half-life shorter than that of other VZV glycoproteins including gB, gE and gH (Virology (2007) 358, 283-90 and Journal of Virolology (1999) 73, 4197–4207). Our anti VZV ORF5 antibody VZ5.12 works in ELISA (on immunogen), IF (on VZV infected cells) as well as is cross-reactive with SVV (Simian Varicella virus) and recognizes the glycosylated mature form of gK in both VZV and SVV. Each LOT of VZ5.12 is validated for Western blot (on VZV infected cell lysates, described in J Virol. 2013 Jun;87(12):6943-54.).
Clone: VZ 5.12
Catalog No.: HR-VZV-01
Host Species: Mouse
Reactivity: Varicella zoster virus
Antigen/Immunogen: The immunogen consisted of full length VZV ORF5 and was produced in E.coli
Tested Applications: ELISA; WB
Varicella zoster virus
The immunogen consisted of full length VZV ORF5 and was produced in E.coli
€120.00 – €500.00
|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 ORF18 (UniProtKB – Q6QCN7) encodes a small subunit of the viral ribonucleotide reductase, which together with the large subunit, encoded by the VZV ORF19, forms the ribonucleotide reductase holoenzyme complex (RNR)
Open reading frame 37 (ORF37) of Varicella zoster encodes for envelope glycoprotein H (gH). VZV gH is a 118kDa type 1 transmembrane glycoprotein highly conserved among other alphaherpesviruses.
VZV ORF23 encodes a 24 kDa small capsid surface protein that localizes primarily to cell nuclei during infection and is not essential for viral replication in cell culture, even though its absence disrupts the capsid assembly.