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SAB4200695

Sigma-Aldrich

Anti-VSV Glycoprotein antibody, Mouse monoclonal

clone P5D4, purified from hybridoma cell culture

Synonyme(s) :

VSV, VSV glycoprotein, Vesicular Stomatitis Virus glycoprotein

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Niveau de qualité

200

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

P5D4, monoclonal

Forme

buffered aqueous solution

Espèces réactives

virus (Vesicular stomatitis virus (VSV))

Conditionnement

antibody small pack of 25 μL

Concentration

~1 mg/mL

Technique(s)

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

Isotype

IgG1

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

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.

Application

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
019M4896V
078M4885V
22180332
018M4841V
057M4842V

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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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