V4388
Anti-VP16 antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti Alpha trans-inducing protein
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IP, WB
Citations:
17
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
technique(s)
immunoprecipitation (IP): 10 μg using mammalian cell extracts expressing VP16 fusion proteins, western blot: 1:1,000 using mammalian cell extracts expressing VP16 fusion proteins
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
Anti-VP16 is produced in rabbit using a synthetic peptide corresponding to amino acids 474-487 of the herpes simplex virus VP16 protein, conjugated to KLH via an N-terminal added cysteine residue. Whole antiserum is fractionated and further purified by ionexchange chromatography to provide the IgG fraction of antiserum that is essentially free of other rabbit serum proteins.
Immunogen
synthetic peptide corresponding to amino acids 474-487 of the herpes simplex virus VP16 protein, conjugated to KLH via an N-terminal added cysteine residue.
Application
Anti-VP16 recognizes VP16 fusion proteins by immunoblotting and immunoprecipitation. It is used to study the effect of sialic acid on herpes simplex virus type 1 envelope glycoproteins. It is also used to study if self-association of lymphocytic choriomeningitis virus nucleoprotein is mediated by its N-terminal region and is not required for its anti-interferon function.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Related Content
Instructions
Jamie Snider et al.
Nature protocols, 5(7), 1281-1293 (2010-07-03)
The biological function of proteins may be predicted by identification of their interacting partners, and one of the major goals of the postgenomic era is the mapping of protein interaction networks. Membrane proteins are of particular interest because of their
Saranya Kittanakom et al.
Biochemical and biophysical research communications, 445(4), 746-756 (2014-02-25)
G-protein coupled receptors (GPCRs) are involved in a variety of disease processes and comprise major drug targets. However, the complexity of integral membrane proteins such as GPCRs makes the identification of their interacting partners and subsequent drug development challenging. A
Jeremy R Teuton et al.
Journal of virology, 81(8), 3731-3739 (2007-01-19)
Herpes simplex virus type 1 (HSV-1) envelope proteins are posttranslationally modified by the addition of sialic acids to the termini of the glycan side chains. Although gC, gD, and gH are sialylated, it is not known whether sialic acids on