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Merck

V4888

Anti-VSV-G antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Vesicular Stomatitis Virus glycoprotein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.56
MDL number:
MFCD00164761
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, IP, WB
Citations:
73

Key Documents

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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

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

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

General description

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.

Immunogen

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)

Biochem/physiol Actions

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.

Physical form

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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Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

V4888-BULK: + V4888-200UG: + V4888-200AMP: + V4888-VAR:

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Certificates of Analysis (COA)

Lot/Batch Number
0000515686
0000515686
0000453928
0000453928
0000414612

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A mechanism for Wnt coreceptor activation
Tamai K, et al.
Molecular Cell, 13(1), 149-156 (2004)
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)
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)
Sven Eyckerman et al.
Nature communications, 7, 11416-11416 (2016-04-29)
Cell lysis is an inevitable step in classical mass spectrometry-based strategies to analyse protein complexes. Complementary lysis conditions, in situ cross-linking strategies and proximal labelling techniques are currently used to reduce lysis effects on the protein complex. We have developed
View All Related Papers

Related Content

Data Sheet - V4888

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