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V4888

Sigma-Aldrich

Anti-VSV-G antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Vesicular Stomatitis Virus glycoprotein

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.56

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

mammals

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 0.5 μg using VSV-G tagged fusion proteins from transfected mammalian cell lysates (tagged fusion proteins from transfected mammalian cell lysates)
indirect immunofluorescence: 1.0 μg/mL using VSV-G tagged fusion proteins in methanol/acetone fixed transiently transfected cells
western blot: 0.1-0.2 μg/mL using VSV-G tagged fusion proteins from transfected mammalian cell lysates

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

The Anti-VSV-G rabbit antibody reacts with amino- and carboxyl-terminal VSV-G tagged fusion proteins.
Vesicular stomatitis viruses (VSV) belongs to the Vesiculovirus genus of the Rhabdoviridae family. Vesicular stomatitis virus G (VSV G) protein is considered to be the early recognized type III viral fusion protein.

Immunogène

synthetic peptide corresponding to amino acids 497-511 (N-Tyr-Thr-Asp-Ile-Glu-Met-Asn-Arg-Leu-Gly-Lys-C) of the Vesicular Stomatitis Virus glycoprotein (VSV-G), conjugated to maleimide activated KLH via a cysteine residue added at the carboxyl terminus. The antibody recognizes the VSV-G tag at both the C-terminus and N-terminus.

Application

Anti-VSV-G antibody produced in rabbit has been used in western blotting and immunoprecipitation.
Antibody is suitable for immunoblotting, immunoprecipitation, and indirect immunofluorescence.
immunocytochemistry.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Chromatin immunoprecipitation (1 paper)
Western Blotting (1 paper)
Western blotting following immunoprecipitation (1 paper)

Actions biochimiques/physiologiques

Vesicular stomatitis virus G (VSV G) is capable of stimulating cell-cell fusion upon low pH stimulation. The transmembrane region of VSV G protein is highly essential for the virus transition from the hemi-fusion to full fusion state.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide as a preservative.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Vesicular stomatitis virus glycoprotein is a determinant of pathogenesis in swine, a natural host
Martinez I, et al.
Journal of virology, 77(14), 8039-8047 (2003)
Periodic fever with aphthous stomatitis, pharyngitis, and cervical adenitis syndrome is associated with a CARD8 variant unable to bind the NLRP3 inflammasome
Cheung MS, et al.
Journal of immunology (Baltimore, Md. : 1950), 198(5), 2063-2069 (2017)
Vesicular stomatitis virus G protein transmembrane region is crucial for the hemi-fusion to full fusion transition
Ci Y, et al.
Scientific Reports, 8(1), 10669-10669 (2018)
A mechanism for Wnt coreceptor activation
Tamai K, et al.
Molecular Cell, 13(1), 149-156 (2004)
Sudha Chugani et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(23), 10673-10678 (2010-05-26)
Pseudomonas aeruginosa quorum control of gene expression involves three LuxR-type signal receptors LasR, RhlR, and QscR that respond to the LasI- and RhlI-generated acyl-homoserine lactone (acyl-HSL) signals 3OC12-HSL and C4-HSL. We found that a LasR-RhlR-QscR triple mutant responds to acyl-HSLs

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