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SensiQ® Semi-automated - Dual Channel SPR

     


bullet on SensiQ: Overview

 

Cost Effective, Surface Plasmon Resonance System for Biomolecular Interaction Analysis

Surface plasmon resonance has proved to be an invaluable tool for scientists involved in characterizing biomolecular interactions for a wide range of research activities such as antibody selection and screening, drug discovery, ligand fishing, binding specificity, and gene regulation. However, researchers have long been dependent on core facilities and centralized labs for access to SPR technology. Now, the ability to perform binding interactions in real time and obtain high quality affinity and kinetic data is available to labs of all sizes in an uncompromised, affordable solution.

SensiQ Explorer is a dual-channel, semi-automated SPR system which utilizes advanced microfluidics, proven surface attachment methodologies, and state-of-the-art data analysis tools to provide kinetic, affinity and concentration data researchers can use with a high degree of confidence. SensiQ has been designed with the end-user in mind through the use of control and data handling wizards to insure ease of operation through the entire experimental processs. With innovative hardware and powerful software tools, SensiQ will set a new standard for biomolecular interaction analysis.
 

bullet on Features


SensiQ features many of the key benefits of more costly instruments and improves upon them in many ways.
  • High quality affinity and kinetic data at an affordable price.
  • Real-time reference subtraction achieved through low dead-volume microfluidics.
  • High mass transport of analyte to the sensor surface using low nanoliter volume flow channels.
  • Easy to use control software utilizing software wizards.
  • Integrated, proven data analysis software based on the Scrubber and Clamp platforms.
  • High sensitivity achieved through a robust, stable design based on Kretschmann optics.
  • Wide variety of surface chemistries available to handle almost any application.
  • Low noise and drift achieved through Peltier temperature control.

bullet on Applications


As a technique for studying biomolecular binding, surface plasmon resonance has been shown to be of great value in a diverse range of research activities including drug discovery, cell signaling, gene regulation, and structure-function studies.

Some of the different types of affinity pairs to be characterized by this technique include:

  • Protein-Protein
  • Protein-DNA
  • Protein-Small Molecule
  • Antibody-Antigen
  • Membrane receptor-Ligand
  • Peptide-Receptor
Kinetics of association and dissociation, affinity constant measurements, concentration determinations and ligand fishing are all examples of the capabilities inherent in SPR and SensiQ provides this valuable data in an easy to use, affordable instrument.
 

bullet on Specifications

 
Technical Specifications
Real time reference curve subtraction
Yes
Channel to channel dead volume
< 60nl
Flow cell volume
10 to 250µl
Refractive index range
1.33-1.40
Short time noise
< 0.25RU
Long term noise
< 0.40RU/min
Flow rate
5-150 µl/min
Sample loading
manual (syringe)
Sample inject
automatic
Temperature control
15°-40°C; (+15° / -5° from ambient)
Working Ranges
ka
1 x 108M-1s-1
kd
10-1-10-6s-1
Concentration
~10-3 - 10-11M
KD
~10-4 - 10-11



 bullet on Surface Chemistries

ICx Nomadics Recommendation for Kinetic Analysis Applications - We recommend two dimensional surface chemistry for kinetic applications as the interpretation of kinetic constants is simplified.

  1. Gold Only Surface

    Sensor provided with gold coated glass surface with no further modification to facilitate the attachment of user-developed functional chemistry.

  2. COOH1

    The COOH1 surface is a two dimensional carboxylated coating suitable for a wide variety of biomolecular interactions. This surface has proven to resist non-specific binding better than any other coating by taking advantage of the chemical properties of polyethylene glycol (PEG). Coupling of ligands to this surface is normally achieved via amine coupling (EDC/NHS chemistry) but alternative methods such as thiol coupling, disulfide exchange and hydrazide coupling may also be employed.

  3. COOH2

    The COOH2 surface is a short carboxylated polysaccaride coating suitable for a wide variety of biomolecular interactions. This surface is similar to COOH1 in charge potential but is more favorable in some applications as polysaccaride has different characteristics. The same coupling chemistries can be used with the COOH2 surface as with COOH1 surface.

  4. BioCap

    The BioCap surface is a two dimensional coating that utilizes the high affinity biotin – avidin interaction as the basis for ligand immobilization. A deglycosylated variant of avidin is covalently coupled to the BioCap surface; making it ideal for the capture of biotinylated reagents including peptides, oligonucleotides, proteins and sugars in a non-reversible manner.

  5. VesCap & VesHiCap

    The VesCap surface is a two dimensional chemistry for the immobilization of vesicles. Liposomes, unilamellar vesicles and even crude membrane preparations may be conveniently immobilized in a single step. A hydrocarbon chain is presented on this surface as an ‘anchor’ to hold the hydrophobic portion of the membrane to the surface. Components embedded in the vesicles will continue to diffuse and this property makes this surface ideal for membrane bound receptor studies.

  6. HisCap

    The HisCap surface is a two dimensional chemistry for the reversible immobilization of His-tagged ligands. This surface is ideal for capture of polyhistidine-tagged recombinant proteins. Immobilized proteins may be removed by exposure to free imidazole allowing the surface to be re-coated and reused.

  7. HiCap

    The HiCap surface is a three dimensional polysaccaride chemistry that is ideal for amine coupling of small peptides, drugs and other small molecules that possess amine groups. Such biomolecules show negligible preconcentration and must be exposed to the surface at high concentrations. This surface is uncharged and confers high resistance to non-specific binding. Very high binding capacities may be achieved using standard coupling chemistries such as CDI.

  8. AvHiCap

    The AvHiCap surface is a three dimensional polysaccaride coating utilizing biotin to capture avidin-conjugated ligands. It is non-charged thereby limiting non-specific binding and making this surface ideal for acidic proteins. This surface consists of a large polysaccaride hydrogel and is useful where high binding capacity is required.

  9. AvCap

    The AvCap surface is a two dimensional coating utilizing biotin to capture avidin-conjugated ligands. It can reversibly bind a full monolayer of protein via the strong affinity that exists between biotin and the four binding sites of avidin, streptavidin and their derivatives. Avidin bound to a planar layer of biotin can be used to capture another biotinylated ligand using one of the other available sites. A solution of guanidine-HCl may be used to denature the protein leaving the surface-bound biotin residues free to recapture fresh conjugates.

  10. COOH 3

    The COOH3 surface is identical to the COOH1 surface but is engineered to possess a far lower density of carboxylic acid groups. This lower capacity surface is tailored for kinetic applications where low binding capacity is required, but its greatest strength is in the reduced non-specific binding that results from the reduced electrostatic potential.

  11. COOH 4

    The COOH4 surface is a non-planar version of the COOH1 sensing surface that enables higher ligand capacity by using a thin hydrophilic film of folded aggregates that are embedded into the surface. The COOH4 surface is recommended when the analyte binding response is expected to be too low. Although increased baseline noise is expected with COOH4, the ligand loading capacity may be expected to increase by a factor of 3-5 fold. We advise trying the COOH1 or COOH2 surface chemistries before deciding to try the COOH4.