The next generation of LRC-TriCEPS
Now available
TriCEPS v.3.0 enables receptor identification for your orphan ligands at the surface of living cells without genetic manipulation. Key features of the new TriCEPS v.3.0 and LRC- TriCEPS technology are:
- Reduction of the number of cells needed:
- TRICEPS v.3.0 LRC experiments require 5-10 fold less starting material for successful receptor identification compared to TRICEPS v.2.0.
- High coverage of the surfaceome.
- A modified LRC workflow enabled by TriCEPS v.3.0 allows for the theoretical identification of up to 85% of all putative cell surface proteins.
- Identification of N-, C-, O- glycosylated targets
More sensitive identification of low copy number cell surface receptors through whole protein pull-down.
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Decoding the extracellular interactome using LRC-TriCEPS
Ligand-receptor capture
The LRC-TriCEPS technology was invented by Andreas Frei and Bernd Wollscheid from ETH Zurich who published the technology in Nature Biotechnology Nature Biotechnology (Frei et al.(2012) Nature Biotechnology 30:997-1001) and further developed it to HATRIC-LRC (Sobotzki et al. Nature Communications, volume 9, Article number: 1519 (2018) doi:10.1038/s41467-018-03936-z)
Orphan ligands:
- Extracellular proteins
- Peptide ligands
- Antibodies
- Viruses
- Engineered affinity binders
Dualsystems Biotech AG is a biotech company providing analytic services for protein-protein interactions.
If you are looking for the targets of your ligand – peptide, protein, antibody, and virus – that are relevant in the living organism, call us on +41 44 738 50 00 or fill in the form on the right hand. We will contact you to see how LRC-TriCEPS technology (ligand-receptor capture) can answer your questions.
LRC-TriCEPS is a novel approach enabling the identification of cell surface receptors and off-targets on living cells for a wide range of orphan ligands. Advantages of LRC-TriCEPS compared to other approaches:
- No genetic manipulation
- No hypothesis needed
- Targets are embedded in plasma membrane in their natural microenvironment
- Cells are alive during interaction
Availability
The TriCEPS-based ligand-receptor capture technology is now available at Dualsystems.
LRC-TriCEPS is a novel approach enabling the identification of cell surface receptors and off-targets on living cells for a wide range of orphan ligands, such as:
- Peptides
- Protein
- Antibodies
- Engineered affinity binders
- Viruses
Availability
The TriCEPS™-based ligand-receptor capture technology is now available.
Principle of LRC-TriCEPS
LRC-TriCEPS is a fast and sensitive approach to discover cell surface N-, C-, and O-glycosylated receptors for a ligand of interest.
- Label ligand with the TriCEPS™ chemoproteomic reagent
- Activate target cells or native tissue to oxidize cell surface glycans
- Incubate ligand-TriCEPS™ complex with activated cells
- TriCEPS™ immediately links ligand and cognate receptor(s)
- Isolate all membrane proteins with the support of TriCEPS
- Tryptic digest of all membrane proteins
- Identification of peptides by mass spectrometry
- Analysis of data using statistics and bioinformatics
LRC-TriCEPS – a trifunctional chemoproteomics reagent
TriCEPS™ structure:
- NHS-ester for attachment to the ligand
- Protected hydrazine function for capturing the interacting receptor
- Pull out function for purification of ligand-receptor peptides
Requirements
Requirements for one LRC experiment: Ligand in triplicate compared to control in triplicate
- 300 µg ligand containing a free amino group
- 60 Mio cells or 50 µm tissue slice
LRC-TRICEPS SERVICES
Identification of the targets and off targets at the cell surface on the living cells
LRC-TriCEPS / HATRIC-LRC Publications
Concerning the LRC-TriCEPS or HATRIC-LRC platforms.
Acidity changes immunology: a new VISTA pathway
Nature Article VISTA interaction with PSGL-1 identified by LRC-TriCEPS
Anti-VISTA antibody that inhibits Vista function and blocks interaction with PSGL-1 and VSIG3 proteins slows tumor growth
Phage resistance at the cost of virulence
PLOS Pathogens | https://doi.org/10.1371/journal.ppat.1008032 October 7, 2019
White Paper Ligand-Receptor Identification Methodologies Details Matter
Validation of extracellular ligand–receptor interactions by Flow‑TriCEPS
Cardiac Targeting Peptide, a Novel Cardiac Vector: Studies in Bio-Distribution, Imaging Application, and Mechanism of Transduction
Leukocyte differentiation by histidine-rich glycoprotein/stanniocalcin-2 complex regulates murine glioma growth through modulation of anti-tumor immunity
Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions
HATRIC-based identification of receptors for orphan ligands
Staphylococcal Superantigens Use LAMA2 as a Coreceptor GPCT signaling To Activate T Cells
Toll like receptors TLR1/2, TLR6 and MUC5B as binding interaction partners with cytostatic proline rich polypeptide 1 in human chondrosarcoma
Phenotypic screening—the fast track to novel antibody discovery
Identification of Putative Receptors for the Novel Adipokine CTRP3 Using Ligand-Receptor Capture Technology
Serum stimulation of CCR7 chemotaxis due to coagulation factor XIIa-dependent production of high-molecular-weight kininogen domain 5
Laminin targeting of a peripheral nerve-highlighting peptide enables degenerated nerve visualization
Identification of cell surface receptors for the novel adipokine CTRP3
Dilp8 requires the neuronal relaxin receptor Lgr3 to couple growth to developmental timing
- Received:
- Accepted:
- Published online:
A Mass Spectrometric-Derived Cell Surface Protein Atlas
Protter
Ligand-based receptor identification on living cells and tissues using TRICEPS
Flex your TRICEPS
Customers Testimonials – LRC-TriCEPS Service
Testimonials from our customers who have used the LRC-TriCEPS technology – in collaboration with Dualsystems Biotech AG.
LRC-TriCEPS customers worldwide
Over 200 satisfied customers from 28 countries.
- Extracellular proteins
- Peptide ligands
- Antibodies
- Engineered affinity binders
- Viruses
- Small molecules
- Extracellular proteins
- Peptide ligands
- Antibodies
- Engineered affinity binders
- Viruses