Herpes simplex Virus 1 VP21/VP22a antibody | LP13
Mouse anti Herpes simplex Virus 1 VP21/VP22a
- Product Type
- Monoclonal Antibody
- Herpes simplex Virus 1 VP21/VP22a
|Mouse anti Herpes simplex Virus 1 VP21/VP22a antibody, clone LP13 recognizes Herpes simplex virus 1, also known as HSV-1, a member of the herpes virus family, Herpesviridae that infect humans. HSV-1 is contagious and symptoms of infection include watery blisters in the skin or mucous membranes of the mouth, lips or genitals.
Clone LP13 binds to the HSV-1 VP21/VP22a scaffold proteins.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- <0.1% Sodium Azide (NaN3)
- HSV-1 strain HFEM
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice were fused with cells of the NS1 mouse myeloma cell line.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
References for Herpes simplex Virus 1 VP21/VP22a antibody
Gao, M. et al. (1994) The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growth.
J Virol. 68 (6): 3702-12.
Yang, K. et al. (2009) The putative leucine zipper of the UL6-encoded portal protein of herpes simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their association with capsids.
J Virol. 83 (9): 4557-64.
McCann 3rd P.J.et al. (1994) Investigation of the specificity of the herpes simplex virus type 1 protease by point mutagenesis of the autoproteolysis sites.
J Virol. 68 (1): 526-9.
Spencer, J.V. et al. (1997) Structure of the herpes simplex virus capsid: peptide A862-H880 of the major capsid protein is displayed on the rim of the capsomer protrusions.
Virology. 228: 229-35.
Mcnab, A.R. et al. (1998) The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.
J Virol. 72 (2): 1060-70.
Morioka, H. et al. (1999) Co-localization of HSV-1 DNA and ICP35 protein by in situ hybridization and immunocytochemistry.
J Electron Microsc (Tokyo). 48: 621-8.
Newcomb, W.W. et al. (2000) Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.
J Virol. 74 (4): 1663-73.
Preston, V.G. and McDougall, I.M. (2002) Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.
J Virol. 76: 673-87.
View The Latest Product References
Mcclelland, D.A. et al. (2002) pH reduction as a trigger for dissociation of herpes simplex virus type 1 scaffolds.
J Virol. 76 (15): 7407-17.
Yang, K. et al. (2007) Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus.
J Virol. 81 (12): 6419-33.
Bucks, M.A. et al. (2007) Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids.
Virology. 361: 316-24.
Roller, R.J. et al. (2011) Intragenic and Extragenic Suppression of a Mutation in Herpes Simplex Virus 1 UL34 That Affects both Nuclear Envelope Targeting and Membrane Budding.
J Virol. 85: 11615-25.
Vu, A. et al. (2016) Extragenic Suppression of a Mutation in Herpes Simplex Virus 1 UL34 That Affects Lamina Disruption and Nuclear Egress.
J Virol. 90 (23): 10738-51.
Feutz, E. et al. (2019) Functional interactions between herpes simplex virus pUL51, pUL7 and gE reveal cell-specific mechanisms for epithelial cell-to-cell spread.
Virology. 537: 84-96.
Yang, K. and Baines, J.D. (2009) Tryptophan residues in the portal protein of herpes simplex virus 1 critical to the interaction with scaffold proteins and incorporation of the portal into capsids.
J Virol. 83: 11726-33.
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