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V4388

Sigma-Aldrich

Anti-VP16 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(e):

Anti Alpha trans-inducing protein

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About This Item

MDL-Nummer:
MFCD02264216
UNSPSC-Code:
12352203
NACRES:
NA.56

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Methode(n)

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

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Verwandte Kategorien

Allgemeine Beschreibung

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.

Anwendung

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.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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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
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
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
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
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