Datasheet

生物学的記述

Specificity	VSV-G tag Antibody [N12B16] detects recombinant proteins containing the VSV-G epitope tag.
Background	The VSV-G tag is a short, highly immunogenic epitope (sequence: QMRTRRHLHV) derived from the membrane-proximal C-terminal region of vesicular stomatitis virus glycoprotein (VSV-G), a class III viral fusion protein belonging to the rhabdovirus glycoprotein family. The native VSV-G ectodomain folds into three conserved domains: a fusion domain (FD) with membrane-interacting loops (residues ~118-136), pleckstrin homology domain (PHD), and trimerization domain (TrD), connected by flexible hinge regions (R1-R5) that undergo pH-induced refolding; the tag corresponds to a linear, solvent-exposed antigenic site in the post-fusion conformation recognized by neutralizing antibodies like PIV. When fused to recombinant proteins, the small VSV-G tag (11 amino acids) minimally perturbs native folding and enables sensitive detection via commercial monoclonal antibodies in immunoblotting, immunoprecipitation, immunofluorescence, and flow cytometry without affecting subcellular localization or interactions. Native VSV-G mediates broad receptor binding (e.g., LDL-R, CR2/CR3 domains via basic residues H8, K47, R354), clathrin-mediated endocytosis, and low-pH-triggered fusion through irreversible trimer rearrangement, underpinning its use in pseudotyping lentiviral/retroviral vectors for stable, high-titer gene delivery across diverse cell types with no disease relevance as a tag.

Specificity

VSV-G tag Antibody [N12B16] detects recombinant proteins containing the VSV-G epitope tag.

Background

The VSV-G tag is a short, highly immunogenic epitope (sequence: QMRTRRHLHV) derived from the membrane-proximal C-terminal region of vesicular stomatitis virus glycoprotein (VSV-G), a class III viral fusion protein belonging to the rhabdovirus glycoprotein family. The native VSV-G ectodomain folds into three conserved domains: a fusion domain (FD) with membrane-interacting loops (residues ~118-136), pleckstrin homology domain (PHD), and trimerization domain (TrD), connected by flexible hinge regions (R1-R5) that undergo pH-induced refolding; the tag corresponds to a linear, solvent-exposed antigenic site in the post-fusion conformation recognized by neutralizing antibodies like PIV. When fused to recombinant proteins, the small VSV-G tag (11 amino acids) minimally perturbs native folding and enables sensitive detection via commercial monoclonal antibodies in immunoblotting, immunoprecipitation, immunofluorescence, and flow cytometry without affecting subcellular localization or interactions. Native VSV-G mediates broad receptor binding (e.g., LDL-R, CR2/CR3 domains via basic residues H8, K47, R354), clathrin-mediated endocytosis, and low-pH-triggered fusion through irreversible trimer rearrangement, underpinning its use in pseudotyping lentiviral/retroviral vectors for stable, high-titer gene delivery across diverse cell types with no disease relevance as a tag.

使用情報

Application

WB, IHC, IF, FCM

Dilution

WB	IHC	IF	FCM
1:1000	1:5000	1:2000	1:500

Reactivity

Source

Rabbit Monoclonal Antibody

MW

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/20921141/
https://pubmed.ncbi.nlm.nih.gov/18345480/

VSV-G tag Antibody [N12B16]

生物学的記述

使用情報

References

Application Data