A1970
Anti-VSV-Glycoprotein−Agarose antibody, Mouse monoclonal
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
Conjugate:
agarose conjugate
Clone:
P5D4, monoclonal
Application:
IP, protein purification
Citations:
7
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
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.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunoprecipitation (1 paper)
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.
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
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.
A1970-1ML: + A1970-BULK: + A1970-VAR:
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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
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
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
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
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
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