VZV ORF11 encodes a tegument protein, an orthologue of HSV1 protein UL47 which is highly conserved among alphaherpesviruses. Che et al. used deletion mutant to show that ORF11 an important VZV virulence determinant for skin (J. Virol. 82, 5825–5834 (2008).). Only rabbit sera was available to analyze the ORF11 before we generated VZV mAbeom. Our anti-VZV11 antibody VZ 11N.12 shows that during infection VZV ORF11 protein localizes to Golgi network. Our anti-VZV11 antibody VZ 11N.12 works in ELISA (on immunogen), IF (on VZV infected cells) and each LOT is validated for Western blot of VZV infected lysates, where itrecognizes a protein of ~110 kDa (described in J Virol. 2013 Jun;87(12):6943-54.).
Clone: VZ 11N.12
Catalog No.: HR-VZV-07
Host Species: Mouse
Reactivity: Varicella zoster virus
Antigen/Immunogen: The immunogen consisted of ORF11 N terminal domain (amino acids 1-400) and was produced in E.coli
Tested Applications: ELISA; IF; WB
Recommended Dilution: n/a
Varicella zoster virus
The immunogen consisted of ORF11 N terminal domain (amino acids 1-400) 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 ORF27 encodes a nuclear egress lamina protein, that together with the nuclear egress membrane protein encoded by the product of VZV ORF27, most likely plays a role in the egress of assembled viral capsids from the nuclei of VZV infected cells to the cytoplasm.
The ORF50 gene of the varicella-zoster virus (VZV) encodes glycoprotein M which is conserved among all herpesviruses. VZV gM is predicted to be an eight-transmembrane envelope glycoprotein modified with a complex N-linked oligosaccharide.
ORF48 encodes an alkaline nuclease (J Virol. 87: 11936-11938). ORF48 protein is homologous to herpes simplex type 1 (HSV-1) UL12, human cytomegalovirus (hCMV) UL98 and Epstein Barr virus (EBV) BGLF5.
Immediate-early 62 protein (IE62) is a homolog of herpes simplex type 1 (HSV-1) ICP4. These two proteins have conserved DNA bidnding domain,while not activation domain (J Virol 1993. 67: 4246-4251).