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SAB4200695

Sigma-Aldrich

Anti-VSV Glycoprotein antibody, Mouse monoclonal

clone P5D4, purified from hybridoma cell culture

Synonym(s):

VSV, VSV glycoprotein, Vesicular Stomatitis Virus glycoprotein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

200

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

P5D4, monoclonal

form

buffered aqueous solution

species reactivity

virus (Vesicular stomatitis virus (VSV))

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

immunoblotting: 0.5-1 μg/mL using whole extract of human HEK-293T cells over-expressing Vinculin with VSV-G tagged fusion protein.
immunocytochemistry: suitable
immunofluorescence: 5-10 μg/mL using COS7 cells over-expressing Vinculin with VSV-G tagged fusion protein.
immunoprecipitation (IP): suitable

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

Anti-VSV Glycoprotein antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma P5D4 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide of Vesicular Stomatitis Virus Glycoprotein (VSV-G), conjugated to KLH.

Application

Anti-VSV Glycoprotein antibody, Mouse monoclonal has been used in immunoblotting, immunofluorescence, immunoprecipitation, immunocytochemistry, transmission electron microscopy (TEM) and studies applying microinjection of the antibody.

Biochem/physiol Actions

Vesicular Stomatitis Virus Glycoprotein (VSV-G) constitutes an attractive model to study maturation and intracellular transport of membrane proteins. It mediates attachment of VSV to the cell surface and induces pH-dependent fusion between viral and target membranes. In addition, it possesses information for intracellular sorting in its cytoplasmic domain, including efficient export from the endoplasmic reticulum (ER), basolateral delivery and endocytosis. The unidirectional transport between golgi cisternae was demonstrated using golgi membranes containing VSV-G. Temperature sensitive mutants of VSV-G are used to study exit of folding intermediates from the endoplasmic reticulum.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Karen Geoffroy et al.
Molecular therapy. Oncology, 32(3), 200826-200826 (2024-07-15)
Therapy-resistant ovarian cancers have a poor prognosis and novel effective treatment options are urgently needed. In this study, we evaluated the therapeutic efficacy of the oncolytic vesicular stomatitis virus (VSV) against a panel of patient-derived ovarian cancer cell lines of
Jinghong Xu et al.
Scientific reports, 13(1), 14041-14041 (2023-08-29)
The BCL-2 family protein BCL-RAMBO, also known as BCL2-like 13, anchors at the outer mitochondrial membrane and regulates apoptosis, mitochondrial fragmentation, and mitophagy. However, the mechanisms underlying the proapoptotic role of BCL-RAMBO remain unclear. In the present study, we demonstrated
Auto-regulation of secretory flux by sensing and responding to the folded cargo protein load in the endoplasmic reticulum
Subramanian A, et al.
Cell, 176(6), 1461-1476 (2019)
p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein
Sevier CS and Machamer CE
Biochemical and Biophysical Research Communications, 287(2), 574-582 (2001)
Eric Barklis et al.
The Journal of biological chemistry, 296, 100340-100340 (2021-01-31)
The lipid composition of HIV-1 virions is enriched in sphingomyelin (SM), but the roles that SM or other sphingolipids (SLs) might play in the HIV-1 replication pathway have not been elucidated. In human cells, SL levels are regulated by ceramide
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