Biolayer Interferometry (BLI)
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The Octet RED384 and BLItz instruments from Sartorius detect Biolayer Interferometry, an optical technique used to measure binding kinetics and binding equilibrium.
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12 results for "Biolayer Interferometry"
12 results for "Biolayer Interferometry"
I want to measure a Kd, how do I choose which technique is best?
FAQ
The CMI has four primary technologies to quantify molecular interactions: Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI), Isothermal Titration Calorimetry (ITC) and MicroScale Thermophoresis (MST). Each technologies has its advantages...
Measuring Molecular Interactions
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A wide array of biomolecular interactions from protein/protein interactions to small molecule ligand/compound binding interactions are important in biology. Fundamentally, there are two ways to measure (or quantify) binding of any of these interactions...
Exifone Is a Potent HDAC1 Activator with Neuroprotective Activity in Human Neuronal Models of Neurodegeneration
Journal Article
Genomic instability caused by a deficiency in the DNA damage response and repair has been linked to age-related cognitive decline and neurodegenerative diseases. Preventing genomic instability that ultimately leads to neuronal death may provide a broadly...
Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy
Journal Article
Botulinum neurotoxins (BoNTs) are a family of bacterial toxins with seven major serotypes (BoNT/A-G). The ability of these toxins to target and bind to motor nerve terminals is a key factor determining their potency and efficacy. Among these toxins, BoNT...
For a kinetic binding assay using Surface Plasmon Resonance (SPR) or Biolayer Interferometry (BLI), how do I chose which of my binding partners to immobilize?
FAQ
The relative size of the molecules isn't generally the deciding factor. Large proteins will typically give larger signals, but that isn’t necessarily better.
For protein/protein interactions, start by considering other properties of the proteins. Most...
Center for Macromolecular Interactions
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The Center for Macromolecular Interactions The Center for Macromolecular Interactions (CMI) in the department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School has a mission to enhance basic research in the HMS community by...
Grant Support
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Active and potential CMI users and labs may request a letter of support for grant applications, from the CMI Core director, Kelly Arnett . New users should contact the CMI to discuss you project and getting started at the CMI. Existing CMI user labs may...
To measure a molecular interaction, how do you choose which molecule to be kept at a fixed concentration and which to vary in concentration?
FAQ
The choice of which molecule to keep constant and which to vary will depend on the experiment type, the properties of the molecules and the stoichiometry of the interaction.
For ITC, where neither protein is labeled or immobilized, either molecule can be...
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Data Management
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About CMI Data Files Users are responsible for storage of all raw and processed data collected at the CMI. Users should have a plan to copy or transfer all raw and process data to their own local or cloud storage system. While the CMI allows temporary...