Herpes simplex Virus 1 VP21/VP22a antibody | LP13
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
0.09% Sodium Azide
- 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.
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 12 months from date of despatch
- For research purposes only
Applications of Herpes simplex Virus 1 VP21/VP22a antibody
|Application Name||Verified||Min Dilution||Max Dilution|
Secondary Antibodies Available
Application Based External Images
Product Specific References
References for Herpes simplex Virus 1 VP21/VP22a antibody
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. (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.
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.
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.
MccannPj3, r.d. 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.
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.
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.
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.
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.
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.
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.
Spencer, J.V. et al. (1007) 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.
Vu, A. et al. (2016) Extragenic Suppression of a Mutation in Herpes Simplex Virus Type 1 (HSV-1) UL34 That Affects Lamina Disruption and Nuclear Egress.
J Virol. Sep 21. pii: JVI.01544-16. [Epub ahead of print]
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.