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V5507

Monoclonal Anti-VSV Glycoprotein antibody produced in mouse

clone P5D4, ascites fluid

Synonym(s):

Monoclonal Anti-VSV Glycoprotein

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About This Item

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
P5D4, monoclonal
Application:
immunocytochemistry
immunoprecipitation (IP)
western blot
Technique(s):
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 1:100,000 using whole cell extracts expressing VSV-G tagged fusion protein
Citations:
96
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Product Name

Monoclonal Anti-VSV Glycoprotein antibody produced in mouse, clone P5D4, ascites fluid

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

P5D4, monoclonal

contains

15 mM sodium azide

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 1:100,000 using whole cell extracts expressing VSV-G tagged fusion protein

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

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Application

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

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.

Disclaimer

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.

Immunogen

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

Preparation Note

For continuous use, store at 2 °C to 8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Solutions at working dilution should be discarded if not used within 12 hours.

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Storage Class

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Xiuran Niu et al.
Cell death & disease, 9(10), 971-971 (2018-09-27)
Chaperone-assisted proteasome degradation of oncogenic protein acts as an upstream signal controlling tumorigenesis and progression. The understanding of the co-regulation of chaperone and oncoprotein of endocytosis pathways is extremely limited. In this study, we showed for the first time that
Eric L Haseltine et al.
Bulletin of mathematical biology, 70(6), 1730-1748 (2008-04-26)
Although many tools of cellular and molecular biology have been used to characterize single intracellular cycles of virus growth, few culture methods exist to study the dynamics of spatially spreading viruses over multiple generations. We have previously developed a method
Jonathan Chow et al.
Cell host & microbe, 22(1), 48-60 (2017-07-14)
Asymptomatic infections often proceed undetected, yet can still prime the host to be sensitive to secondary environmental stress. While the mechanisms underlying disease caused by asymptomatic infections are unknown, it is believed that productive pathogen replication is required. We report
Sanne W A Reulen et al.
BMC biotechnology, 9, 66-66 (2009-07-22)
Classical bioconjugation strategies for generating antibody-functionalized nanoparticles are non-specific and typically result in heterogeneous compounds that can be compromised in activity. Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester, providing a
Yongxiang Zheng et al.
Nucleic acids research, 43(11), e73-e73 (2015-03-15)
With the aim of broadening the versatility of lentiviral vectors as a tool in nucleic acid research, we expanded the genetic code in the propagation of lentiviral vectors for site-specific incorporation of chemical moieties with unique properties. Through systematic exploration

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