SAB4200695
Anti-VSV Glycoprotein antibody, Mouse monoclonal
clone P5D4, purified from hybridoma cell culture
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Synonym(s):
VSV, VSV glycoprotein, Vesicular Stomatitis Virus glycoprotein
UNSPSC Code:
12352203
NACRES:
NA.46
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biological source
mouse
Quality Level
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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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
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)
Qingchen Zhu et al.
The Journal of experimental medicine, 217(7) (2020-04-24)
Ubiquitination is an essential mechanism in the control of antiviral immunity upon virus infection. Here, we identify a series of ubiquitination-modulating enzymes that are modulated by vesicular stomatitis virus (VSV). Notably, TRIM24 is down-regulated through direct transcriptional suppression induced by
Advait Subramanian et al.
Cell, 176(6), 1461-1476 (2019-03-09)
Maintaining the optimal performance of cell processes and organelles is the task of auto-regulatory systems. Here we describe an auto-regulatory device that helps to maintain homeostasis of the endoplasmic reticulum (ER) by adjusting the secretory flux to the cargo load.
Jing Zhang et al.
Nature communications, 13(1), 6007-6007 (2022-10-13)
Virus infection affects cellular proteostasis and provides an opportunity to study this cellular process under perturbation. The proteostasis network in the endoplasmic reticulum (ER) is composed of the calnexin cycle, and the two protein degradation pathways ER-associated protein degradation (ERAD)
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