Herpes simplex Virus 1 VP21/VP22a antibody | LP13
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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.
Clone LP13 binds to the HSV-1 VP21/VP22a scaffold proteins.
Product Details
- Target Species
- Viral
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide - Immunogen
- 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.
Storage Information
- Storage
- 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. - Guarantee
- 18 months from date of despatch.
More Information
- Regulatory
- For research purposes only
Applications of Herpes simplex Virus 1 VP21/VP22a antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| Immuno-electron Microscopy | |||
| Immunofluorescence | |||
| Immunoprecipitation | |||
| Western Blotting |
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
Copyright © 2019 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Application Based External Images
Immuno-electron Microscopy
Immunofluorescence
Immunoprecipitation
Western Blotting
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. -
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. -
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. 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. -
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]
