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Conventional Yeast Platform(No need to send samples to China)
• Yeast Library Construction (In-Gate Technology)
• CrY2H-seq Library Screening
• Gene-centered Y1H (Nuclear System)
• TF-Centered Y1H (Nuclear System)
• Two-Hybrid (Nuclear System)
• Two-Hybrid (Membrane System)
• Three-Hybrid (Nuclear System)
• Abiotic-Stress Resistance Gene Screening
• Peptide Library Screening
Nanobody Platform
• Nanobody Screening (Nuclear System)
AI Screening Protein-Interactins
• AI Screening Digital Library
• VHH Antibody Algorithm and Validation
Physical & Chemical indicators Detection
• Stable Isotopes Detection (¹³C/¹⁵N/¹⁸O/²H, Deuterium/³⁴S)
• Soil General Physical and Chemical indicators Detection
• Plant General Physical and Chemical Indicators Detection
• Plant Elements
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Yeast Two-Hybrid (Nuclear System) Vector Kit
Yeast Two-Hybrid (Membrane System) Vector Kit
Yeast One Hybrid (Gene-centered) Vector Kit
Yeast One Hybrid (TF-Centered) Vector Kit
Yeast Secreted Protein Expression Vector Kit
Yeast Signal Peptide Detection Vector Kit
Yeast Three-Hybrid (Nuclear System) Vector Kit
Yeast Colony Rapid Detection Kit
Yeast Abiotic-Stress Resistance Gene Screening Vector Kit
Saccharomyces cerevisiae Surface Display Vector Kit
Nanobody Screening Vector Kit
Plant Direct PCR Kit
Yeast Plasmid Rapid Extraction Kit (One-step)
Pichia Pastoris Surface Display Kit
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Everyone is searching: Nanoantibody screening
Yeast Two-Hybrid Y2H Mb Y2H for Membrane Proteins
Yeast one-Hybrid Y1H TF-centered YlH Yeast Three-Hybrid Y3H
Abiotic-Stress Resistance Gene Screening
Digital Analog Library Screening
PRODUCTS
Yeast One Hybrid (Gene-Centered) Vector Kit
The Pichia pastoris surface display system primarily utilizes the α-agglutinin system to display foreign proteins on the cell surface. The fusion protein is non-covalently attached to the Pichia pastoris cell wall. After the target protein is expressed with Aga2p, it is secreted into the extracellular space. The Aga2p subunit binds to the Aga1p subunit through two disulfide bonds, and Aga1p is covalently linked to the β-glucan in the yeast cell wall, anchoring it in place.
This kit includes an efficient Yeast lysis buffer, capable of effectively breaking down yeast cell walls in a short time, releasing intracellular proteins, nucleic acids, and other vital biomolecules. Yeast colonies can be directly added to the reagent without tedious pipetting, significantly saving experiment time and enhancing work efficiency. This kit is suitable for the extraction of various yeast plasmids, whether from common Saccharomyces cerevisiae or other specialized strains, ensuring excellent extraction results.
This kit contains a green dye, allowing direct electrophoresis after the reaction, enabling quick amplification of target gene fragments in plants, saving time and effort. The Plant lysis buffer is used to disrupt plant cells. The 2×Plant PCR mix includes PCR buffer, dNTPs, MgCl2, and a hot-start rapid Taq enzyme. Simply add primers and template/plant lysate for amplification, reducing pipetting steps and enhancing stability. The 2×Plant PCR mix also includes stabilizers, maintaining stability even after repeated freeze-thaw cycles. The PCR product has an A overhang at the 3' end, suitable for TA cloning.
The antigen-binding capacity of nanobodies is similar to conventional antibodies for three reasons. First, the complementarity-determining region 3 (CDR3) of nanobodies is similar or even longer than that of human VH domain (variable domain of heavy immunoglobulin chain). Second, nanobodies can form finger-like structures to recognize cavities or hidden epitopes that are not available to mAbs.
The most common yeast display system employs fusion of the protein of interest to the C-terminus of the a-agglutinin mating protein Aga2p subunit, a technology pioneered by Boder and Wittrup. The yeast surface display construct designed for this system includes two epitope tags: a hemagglutinin (HA) tag between Aga2p and the N-terminus of the protein of interest, and a C-terminal c-myc tag.
Saccharomyces cerevisiae belongs to eukaryote, which is closer to the expression system of plants and animals. This expression system includes the following processes: glycosylation, disulfide bond formation, and Post-translational modification of protein folding.
This kit is used to amplify fragments from the yeast genome as well as transformed plasmids. The component contains a visualization green dye, which can directly perform polyacrylamide gel electrophoresis and agarose gel electrophoresis after PCR. The PCR product has A- tailing at the 3' end, which is suitable for TA cloning.
The quality yeast one-hybrid system is a technique developed from the yeast two-hybrid to study DNA-protein interactions and is widely used to study the regulation of gene expression in eukaryotic cells, such as identifying DNA binding sites to discover potential binding protein genes, analyzing DNA binding structural domain information, etc.
TF-centered Y1H (Yeast One-Hybrid Technology), which recognizes transcription factors as its recognition elements, can accurately and efficiently identify transcription factor recognition elements and has a wide range of applications in the study of protein-DNA element interactions.
One of the most important branches of genetic engineering is the expression of recombinant proteins using biological expression systems. Nowadays, different expression systems are used for the production of recombinant proteins including bacteria, yeasts, molds, mammals, plants, and insects.
Currently, the most widely used method for prediction of signal peptide from amino acid sequences is to use software SignalP (Petersen et al., 2011). Yeast signal sequence trap (YSST) is a method that can be used to evaluate the function of predicted signal peptides. This method utilizes the yeast Saccharomyces cerevisiae YTK12 strain and pSUC2 vector in which the pSUC2 vector with fused predicted signal peptide is transformed into yeast.
The customized yeast three-hybrid system is mainly used to study more complex macromolecular interactions including three components, providing a new method for the study of protein-protein-protein, protein-RNA-protein, and protein-small molecule-protein interactions.