Anti-Herpes Simplex Virus Glycoprotein D Antibody, clone LP14

Evaluated by Western Blotting in HEK293T cell lysate transfected with HSV gD.

Western Blotting Analysis: A 1:2,000 dilution of this antibody detected Herpes Simplex Virus Glycoprotein D in HEK293T cell lysate transfected with HSV gD.

Anti-Herpes Simplex Virus Glycoprotein D, clone LP14, Cat. No. MABF1975, is a mouse monoclonal antibody that detects Glycoprotein D of Herpes Simplex Virus and has been tested for use in Inhibition, Immunocytochemistry, and Western Blotting.

Research Category
Inflammation & Immunology

Western Blotting Analysis: A 1:2,000 dilution from a representative lot detected Herpes Simplex Virus Glycoprotein D in lysates from VERO cells transfected with HSV-1.

Western Blotting Analysis: A representative lot detected Herpes Simplex Virus Glycoprotein D in Western Blotting applications (Lau, S.Y., et. al. (2015). Viruses. 7(3):915-38; Zenner, H.L., et. al. (2011). J Virol. 85(16):8012-21; Pawliczek, T., et. al. (2009). J Virol. 83(21):11254-64).

Western Blotting Analysis: A representative lot detected Herpes Simplex Virus Glycoprotein D in Western Blotting applications (Ren, Y., et. al. (2012). J Gen Virol. 93(Pt 2):319-29).

Immunocytochemistry Analysis: A representative lot detected Herpes Simplex Virus Glycoprotein D in Immunocytochemistry applications (Lau, S.Y., et. al. (2015). Viruses. 7(3):915-38).

Inhibition Analysis: A representative lot inhibited the fusion of cells infected with HSV-1. (Minson, A.C., et. al. (1986). J Gen Virol. 67(6); 1001-1013.

Clone LP14 detects glycoprotein D of Herpes Simplex virus.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Herpes Simplex Virus envelope Glycoprotein D (UniProt: Q69091) is also known as gD. The envelope of herpes simplex virus (HSV) is complex and contains at least 10 virus-encoded glycoproteins, some of which mediate virus entry into the host cell. HSV virus enters the cell by first fusing its envelope with a membrane of the host cell. Five viral envelope glycoproteins are reported to be involved in this entry process. Binding of glycoprotein D of HSV to a cell surface receptor is required to trigger membrane fusion during entry into host cells. Glycoproteins C and B promote attachment by interacting with cell surface proteoglycans and then glycoprotein D binds to the herpes virus entry mediator (HVEM) receptor that initiates a process that ultimately leads to glycoprotein B-mediated membrane fusion. Glycoprotein D is synthesized with a signal peptide (aa 1-25) that is subsequently cleaved off. It is a homodimeric protein that contains two zinc-binding sites (aa 64 and 264). The ectodomain region of glycoprotein D contains three sites for the addition of N-linked oligosaccharides (N-CHO) and six cysteine residues arranged into three disulfide bonds. During virion morphogenesis, glycoprotein D probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. (Ref.: Whitbeck JC et al. (1997). J. Virol. 71(8); p. 6083 6093; Nicola, AV et al. (1998). J Virol. 72(5): 3595-3601; Giovine, PD et al. (2011). PLos Pathog. 7(9); e1002277).

~50 and 55 kDa observed; 43.35 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Whole Herpex Simplex Virus 2 (HSV-2).

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG2a in PBS without azide.

Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.