Herpes simplex Virus 1 VP21/VP22a antibody | LP13

Mouse anti Herpes simplex Virus 1 VP21/VP22a

Product Type
Monoclonal Antibody
Clone
LP13
Isotype
IgG2a
Specificity
Herpes simplex Virus 1 VP21/VP22a

Product Code Applications Pack Size List Price Your Price Qty
MCA406
Datasheet Datasheet Datasheet
SDS Safety Datasheet SDS
EM IF IP WB 1 mg loader
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loader
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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.

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
<0.1% Sodium Azide (NaN3)
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.
Regulatory
For research purposes only
Guarantee
12 months from date of despatch

This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.

Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
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.

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References for Herpes simplex Virus 1 VP21/VP22a antibody

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  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.
  9. View The Latest Product References
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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]
  15. 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.
  16. 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.

Immuno-electron Microscopy

Immunofluorescence

Immunoprecipitation

Western Blotting

RRID
AB_322110
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Please Note: All Products are "FOR RESEARCH PURPOSES ONLY"

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