A1970

Anti-VSV-Glycoprotein−Agarose antibody, Mouse monoclonal

Name: Anti-VSV-Glycoprotein−Agarose antibody, Mouse monoclonal
Brand: SIGMA

clone P5D4, purified from hybridoma cell culture, PBS suspension

Synonym(s):

Monoclonal Anti-VSV Glycoprotein

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About This Item

NACRES:

NA.56

UNSPSC Code:

12352203

Product Name

Anti-VSV-Glycoprotein−Agarose antibody, Mouse monoclonal, clone P5D4, purified from hybridoma cell culture, PBS suspension

biological source

mouse

conjugate

agarose conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

P5D4, monoclonal

form

PBS suspension

analyte chemical class(es)

proteins (VSV-G)

technique(s)

immunoprecipitation (IP): suitable
protein purification: suitable

isotype

IgG1

capacity

≥15 nmol/mL, resin binding capacity (VSV-G tagged fusion protein)

shipped in

wet ice

storage temp.

2-8°C

Quality Level

200

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Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunoprecipitation (1 paper)

For immunoprecipitation and affinity purification of VSV-G tagged fusion proteins. The antibody recognizes an epitope containing the five carboxy-terminal amino acids of VSV Glycoprotein.

Biochem/physiol Actions

The antibody recognizes an epitope containing the five carboxy-terminal amino acids of VSV Glycoprotein. In infected cells, the antibody localizes the immature forms of VSV-G in the rough endoplasmic reticulum (RER) and in the cisternae of Golgi complex, as well as mature VSV-G at the cell surface and in the budding virus. The antibody does not stain the secreted form of VSV-G which lacks the membrane and the cytoplasmic domain. This antibody has been used for studies on the role of the cytoplasmic domain on newly-synthesized VSV-G during transfer to the plasma membrane and cell surface, using micro-injected antibody, immunoblotting, immunoprecipitation, immunocytochemistry and immunoelectron microscopy. The antibody has been used for the detection, immunoprecipitation and immunocytochemical staining of exogenously introduced constructs tagged with the carboxyl-terminus of VSV-G. This tag does not interfere with the function of the studied protein and can be specifically recognized by the P5D4 antibody without cross-reaction with any endogenous protein.

General description

Anti-VSV-G Agarose Conjugate is the immunoglobulin fraction of Monoclonal Anti-VSV glycoprotein covalently linked to agarose.

Immunogen

synthetic peptide containing the 15 carboxy-terminal amino acids (497-511) of Vesicular Stomatitis Virus Glycoprotein (VSV-G), conjugated to KLH.

Physical form

Supplied as a suspension (1:1,v/v) of beaded agarose in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative

Preparation Note

Prepared using cyanogen bromide-activated agarose.

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Storage Class

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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NHE3 activity is dependent on direct phosphoinositide binding at the N terminus of its intracellular cytosolic region.

Sachin Mohan et al.

The Journal of biological chemistry, 285(45), 34566-34578 (2010-08-26)

The small intestinal BB Na(+)/H(+) antiporter NHE3 accounts for the majority of intestinal sodium and water absorption. It is highly regulated with both postprandial inhibition and stimulation sequentially occurring. Phosphatidylinositide 4,5-bisphosphate (PI(4,5)P(2)) and phosphatidylinositide 3,4,5-trisphosphate (PI(3,4,5)P(3)) binding is involved with

c-di-GMP heterogeneity is generated by the chemotaxis machinery to regulate flagellar motility.

Bridget R Kulasekara et al.

eLife, 2, e01402-e01402 (2013-12-19)

Individual cell heterogeneity is commonly observed within populations, although its molecular basis is largely unknown. Previously, using FRET-based microscopy, we observed heterogeneity in cellular c-di-GMP levels. In this study, we show that c-di-GMP heterogeneity in Pseudomonas aeruginosa is promoted by

Genome-wide protein-DNA interaction site mapping in bacteria using a double-stranded DNA-specific cytosine deaminase.

Larry A Gallagher et al.

Nature microbiology, 7(6), 844-855 (2022-06-02)

DNA-protein interactions are central to fundamental cellular processes, yet widely implemented technologies for measuring these interactions on a genome scale in bacteria are laborious and capture only a snapshot of binding events. We devised a facile method for mapping DNA-protein

Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange.

Yael Katan-Khaykovich et al.

Proceedings of the National Academy of Sciences of the United States of America, 108(4), 1296-1301 (2011-01-12)

Nucleosome deposition occurs on newly synthesized DNA during DNA replication and on transcriptionally active genes via nucleosome-remodeling complexes recruited by activator proteins and elongating RNA polymerase II. It has been long believed that histone deposition involves stable H3-H4 tetramers, such

H-NS-like proteins in Pseudomonas aeruginosa coordinately silence intragenic transcription.

Andrew M Lippa et al.

Molecular microbiology, 115(6), 1138-1151 (2020-11-28)

The H-NS-like proteins MvaT and MvaU act coordinately as global repressors in Pseudomonas aeruginosa by binding to AT-rich regions of the chromosome. Although cells can tolerate loss of either protein, identifying their combined regulatory effects has been challenging because the

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