Yeast protein tagging vectors for BiFC analysis

This product has 18 kinds of vector products with a substitution module capable of substituting the N-terminus fragment of the yellow fluorescent protein and a substitution module capable of substituting the C-terminus fragment of the yellow fluorescent protein. Therefore, you can experiment by selecting a selection marker that matches purpose. The high-purity, high-concentration plasmid DNA is extracted using the AccuPrep® Nano-Plus Plasmid Midi Extraction Kit. So quality is excellent.

Grouped product items
Product Name Qty
pFA6a-VN173-HIS3MX6 (5 μg) [V-1010-V1]
$30.00
pFA6a-VC155-HIS3MX6 (5 μg) [V-1010-V2]
$30.00
pFA6a-VN173-TRP1 (5 μg) [V-1010-V3]
$30.00
pFA6a-VC155-TRP1 (5 μg) [V-1010-V4]
$30.00
pFA6a-VN173-KanMX6 (5 μg) [V-1010-V5]
$30.00
pFA6a-VC155-KanMX6 (5 μg) [V-1010-V6]
$30.00
pFA6a-HIS3MX6-PGAL1-VN173 (5 μg) [V-1010-V7]
$30.00
pFA6a-HIS3MX6-PGAL1-VC155 (5 μg) [V-1010-V8]
$30.00
pFA6a-TRP1-PGAL1-VN173 (5 μg) [V-1010-V9]
$30.00
pFA6a-TRP1-PGAL1-VC155 (5 μg) [V-1010-V10]
$30.00
pFA6a-KanMX6-PGAL1-VN173 (5 μg) [V-1010-V11]
$30.00
pFA6a-KanMX6-PGAL1-VC155 (5 μg) [V-1010-V12]
$30.00
pFA6a-HIS3MX6-PCET1-VN173 (5 μg) [V-1010-V13]
$30.00
pFA6a-HIS3MX6-PCET1-VC155 (5 μg) [V-1010-V14]
$30.00
pFA6a-TRP1-PCET1-VN173 (5 μg) [V-1010-V15]
$30.00
pFA6a-TRP1-PCET1-VC155 (5 μg) [V-1010-V16]
$30.00
pFA6a-KanMX6-PCET1-VN173 (5 μg) [V-1010-V17]
$30.00
pFA6a-KanMX6-PCET1-VC155 (5 μg) [V-1010-V18]
$30.00

Features and Benefits

  • A powerful tool for studying protein-protein interactions in living cells and analyzing intra-cellular location

  • Simple observation by fluorescence microscope with strong fluorescence emitted during the formation of fluorescence complex

  • Analysis of protein interactions at the genomic level (Capable of covering 93% of the yeast proteome)

  • Easy study of unknown functions and interactions of new proteins

  • Proteinization analysis possible (ubiquitination, sumoylation, neddylation, etc.)

Overview

S. cerevisiae VN-fusion library is a system that allows the interaction of proteins in vivo to be more easily detected through fluorescent signals. It consists of 5,809 VN-tagged Open Reading Frames (ORFs) and 93% of the entire genome of S. cerevisiae. While the VN-fusion library is developed by Dr. Won-Ki Huh of Seoul National University (Korea), Bioneer owns its exclusive business license.

Principle

Bimolecular Fluorescence Complementation (BiFC) Assay

Most biological processes are carried out and regulated by dynamic networks of protein-protein interactions. Therefore, understanding and checking their interactions are necessary processes for understanding the cellular functions of proteins.

Bimolecular fluorescence complementation (BiFC) assays are easy to use when studying protein interactions as their fluorescence signals can be directly measured through a microscope. In the BiFC assay, the protein that exhibits yellow fluorescence ('Venus' in the figure below) is divided into two sections ('VN' and 'VC' in the figure below) to utilize their characteristic which only produces illuminance when those are close to each other by forming a whole fluorescent protein complex.

Shyu et al, 2008

Application

Intracellular localization analyze of protein and protein interactions in cells

Application1

Figure 1. A schematic diagram of a strain that simultaneously expresses Sis1 (VN-tagged Sis1) labeled with VN at its N-terminus and Sis1 (VC-tagged Sis1) labeled with VC at its C-terminus



Application2

Figure 2. A diagram showing Sis1, a Type II HSP40 co-chaperone forming a homodimer by interacting with the HSP70 protein Ssa1(Luke et al., 1991).(Sha et al., 2000).

BiFC (bimolecular fluorescence complementation) signals are clearly identified in the nucleus and cytoplasm, meaning that VN-tagged Sis1 and VC-tagged Sis1 may bind in them. Sis1 protein is already known to be present in the two (Huh et al., 2003), while BiFC signals are not appear in strains expressing either VN-tagged Sis1 or VC-tagged Sis1.

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