Large Molecule Characterization

The 8-channel Octet QKe System Provides Rapid Characterization of Antibodies, Proteins, and Other Large Biomolecules (> 5000 Da)

Monitor binding events in real time to calculate on rates (ka), off rates (kd), and affinity constants(KD).  Screen kinetics of 64 samples in 1.5 hours.

Analyze samples in crude matrix - The fluidics-free Dip and Read technology with samples in a plate format combined with ready-to-use biosensors allows for high flexibility in sample type. Quantitation of 96 samples can be accomplished in 32 minutes.

Versatility to detect a wide range of molecules

Customize your own biosensor chemistries or use ready to use biosensors for a variety of analytes.

Eight parallel, independent channels for maximum speed and flexibility

Each channel is independent of the others allowing for analysis of different sample types simultaneously. Analysis can be done using a single channel or up to eight channels.

Fluidics-free Dip and Read format reduces assay time and maintenance cost

The Octet provides faster time to results and process economy when compared to other technologies due to this format.

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Applications

Kinetic and Affinity Characterization

Octet instruments accurately measure kinetic constants by bringing the detection surface directly to the sample, eliminating the need for microfluidics. With ready to use biosensors for most proteins, the unique Dip and Read approach streamlines workflows and expedites assay development. It allows for direct measurement of crude samples with minimal instrument maintenance.

Protein Quantitation in Bioprocessing

Accurately determining the concentration of antibodies and other proteins is critical to the selection of cell lines for development and the optimization of antibody production. Rapid turnaround time of results improves process efficiencies and productivity that cannot be achieved with existing methods such as HPLC and ELISA.

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Featured Publications

Label-Free Detection Technologies: Key Considerations and Applications

Binding interactions in biological samples are dynamic and driven by changes to the environment. The techniques used to characterize these...

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Technology

Bio-Layer Interferometry (BLI) based on fiber optic biosensors

Sample volume

180–220 µL/well
Nondestructive testing, easily recovered

Data presentation

Sensorgrams displaying kinetic traces or concentration binding rates
Epitope binning and cross-blocking matrices and trace overlays
Tabulated kinetic or concentration data

Automation

Up to 8 assays in parallel; up to 96 assays per 96-well plate

Orbital flow capacity

Static or 100–1500 rpm

Analysis temperature

Ambient + 4°C to 40°C, in 1°C increments

Association rate constant (ka)

102 to 105  M-1 s-1

Dissociation rate constant (kd)

10-5 to 10-2  s-1

Affinity constant (KD)

0.1 mM to 0.1 nM

Baseline noise (RMS)

≤ 8 pm

Baseline drift

< 0.1 nm/hour

Quantitation range

1 µg/mL to 700 µg/mL at low rpm, LOD of 0.05 µg/mL at 1000 rpm

Quantitation precision

≤10%

Weight

54 lb (24.5 kg)

Dimensions (H x W x D)

18.6 in (H) x 17 in (D) x 20.8 in (W)
47 cm (H) x 43 cm (D) x 53 cm (W)

Sample type

Proteins, antibodies, peptides, serum containing media (up to 25%), DMSO containing buffers, virus-like particles, untreated cell culture supernatants and crude cell lysates

Sample plate

Standard, 96-well, black, flat-bottom microplate

Molecular weight detection

>5000 Da


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