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SAB4200695

Sigma-Aldrich

Anti-VSV Glycoprotein antibody, Mouse monoclonal

clone P5D4, purified from hybridoma cell culture

Synonym(e):

VSV, VSV glycoprotein, Vesicular Stomatitis Virus glycoprotein

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.46

Biologische Quelle

mouse

Qualitätsniveau

200

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

P5D4, monoclonal

Form

buffered aqueous solution

Speziesreaktivität

virus (Vesicular stomatitis virus (VSV))

Verpackung

antibody small pack of 25 μL

Konzentration

~1 mg/mL

Methode(n)

immunoblotting: 0.5-1 μg/mL using whole extract of human HEK-293T cells over-expressing Vinculin with VSV-G tagged fusion protein.
immunocytochemistry: suitable
immunofluorescence: 5-10 μg/mL using COS7 cells over-expressing Vinculin with VSV-G tagged fusion protein.
immunoprecipitation (IP): suitable

Isotyp

IgG1

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Allgemeine Beschreibung

Anti-VSV Glycoprotein antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma P5D4 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide of Vesicular Stomatitis Virus Glycoprotein (VSV-G), conjugated to KLH.

Anwendung

Anti-VSV Glycoprotein antibody, Mouse monoclonal has been used in immunoblotting, immunofluorescence, immunoprecipitation, immunocytochemistry, transmission electron microscopy (TEM) and studies applying microinjection of the antibody.

Biochem./physiol. Wirkung

Vesicular Stomatitis Virus Glycoprotein (VSV-G) constitutes an attractive model to study maturation and intracellular transport of membrane proteins. It mediates attachment of VSV to the cell surface and induces pH-dependent fusion between viral and target membranes. In addition, it possesses information for intracellular sorting in its cytoplasmic domain, including efficient export from the endoplasmic reticulum (ER), basolateral delivery and endocytosis. The unidirectional transport between golgi cisternae was demonstrated using golgi membranes containing VSV-G. Temperature sensitive mutants of VSV-G are used to study exit of folding intermediates from the endoplasmic reticulum.

Physikalische Form

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

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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C Hammond et al.
The Journal of cell biology, 126(1), 41-52 (1994-07-01)
Proteins synthesized in the ER are generally transported to the Golgi complex and beyond only when they have reached a fully folded and assembled conformation. To analyze how the selective retention of misfolded proteins works, we monitored the long-term fate
T E Kreis et al.
Cell, 46(6), 929-937 (1986-09-12)
Using ts045, a temperature sensitive strain of Vesicular stomatitis virus, we show that oligomerization of G protein is a prerequisite for its transport from RER to the Golgi apparatus and for its subsequent maturation. While wild-type G forms an oligomer
T Soldati et al.
Cell, 66(2), 277-289 (1991-07-26)
The isoprotein-specific intracompartmental sorting of the three essential myosin light chains (LCs), the skeletal muscle LC-1f and LC-3f and the nonmuscle LC-3nm, was investigated. Epitope tagging was used to monitor the intracellular localization to different cytoskeletal structures of the exogenously
p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein
Sevier CS and Machamer CE
Biochemical and Biophysical Research Communications, 287(2), 574-582 (2001)
C S Sevier et al.
Molecular biology of the cell, 11(1), 13-22 (2000-01-19)
The vesicular stomatitis virus (VSV) G protein is a model transmembrane glycoprotein that has been extensively used to study the exocytotic pathway. A signal in the cytoplasmic tail of VSV G (DxE or Asp-x-Glu, where x is any amino acid)
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