V4388
Anti-VP16 antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
别名:
Anti Alpha trans-inducing protein
产品名称
Anti-VP16 antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
target post-translational modification
unmodified
biological source
rabbit
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
Quality Level
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
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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
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
Lei Guo et al.
PloS one, 7(9), e45749-e45749 (2012-10-03)
ICP22 is a multifunctional herpes simplex virus 1 (HSV-1) immediate early protein that functions as a general repressor of a subset of cellular and viral promoters in transient expression systems. Although the exact mechanism of repression remains unclear, this protein
Roberto Alfonso-Dunn et al.
Cell host & microbe, 21(4), 507-517 (2017-04-14)
The cellular transcriptional coactivator HCF-1 is required for initiation of herpes simplex virus (HSV) lytic infection and for reactivation from latency in sensory neurons. HCF-1 stabilizes the viral Immediate Early (IE) gene enhancer complex and mediates chromatin transitions to promote
Ying-Hsiu Su et al.
Journal of virology, 80(23), 11589-11597 (2006-09-22)
Following infection, the physical state of linear herpes simplex virus (HSV) genomes may change into an "endless" or circular form. In this study, using Southern blot analysis of the HSV genome, we provide evidence that immediate-early protein ICP4 is involved
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