The six basic research departments at the University of Miami, Miller School of Medicine carry out a broad range of basic science studies with strong translational components. Interdepartmental structures like the Comprehensive Cancer Center which contributes to the maintenance of the proposed SPR equipment foster interactions between basic researchers and with clinical research groups. Among this combined group of researchers including one user from the neighboring Florida Scripps Institute , a strong need exists for modalities that allow highly sensitive and label free molecular interaction studies with small sample volumes. Surface Plasmon Resonance has become a major, if not the dominant, method of analysis for this type of applications in the last decade, especially with its increase in sensitivity in recent years which now includes the label free binding studies of small molecule analytes and the ability to multiplex and automate measurements.

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Surface Plasmon Resonance Spectroscopy is a technique that allows the real-time and label-free measurement of biomolecular interactions, such as. The Biacore T system combines surface plasmon resonance with sensor chip technology to monitor the interaction between molecules in real time. To study the interaction between two binding partners, one interaction partner the so-called ligand is attached to the surface of a sensor chip and the other one the so-called analyte is passed over the surface in a continuous flow of sample solution.

Binding of molecules to the sensor surface generates a signal response that is proportional to the mass of bound molecules and can be detected down to changes of a few pictograms or less per square millimetre on the sensor surface, corresponding to concentrations in the picomolar to nanomolar range in the sample solution.

The detection principle does not require any of the interactants to be labelled, thus, biomolecules can be analysed in their native state. The Biacore T system in our facility delivers high quality kinetic, affinity, concentration, specificity, selectivity, comparability and thermodynamic interaction data. It has a capacity of up to samples including an autosampler that allows unattended operation.

Extraordinary sensitivity makes it possible to work with a sample concentration of as little as 1 pM and up to 2 mM. The affinity range lies between 10 fM and 1 mM. Surface plasmon resonance occurs when plane-polarized light hits a metal film at the interface of media with different refractive indices. When polarized light is directed towards a prism on a sensor chip with a thin metal film on top e. At a certain angle of incidence, the light will excite surface plasmons, causing a dip in the intensity of the reflected light.

Photons of plane-polarized light can interact with the free electrons of the metal layer, inducing a wave-like oscillation of the free electrons, thereby reducing the reflected light intensity. The angle at which the maximum loss of the reflected light intensity occurs is called resonance angle or SPR angle.

While the refractive index at the prism is not changing, the refractive index in the immediate vicinity of the metal surface will change when accumulated mass such as proteins adsorb on it.

The change in refractive index at the surface of the metal film will cause a shift of the SPR angle. Search for:.


Biacore T200

Enjoy Free Shipping on most orders placed online — Terms Apply. Biacore T is a versatile system for high-quality characterization of molecular interactions, all the way from research to discovery and quality control. Biacore T is a versatile system for high-quality characterization of molecular interactions, from ions to viruses. Biacore T software offers a range of tools for confident and reliable kinetic analyses. These analyses can be performed using a multicycle approach many samples against one ligand or when different ligands are immobilized , or alternatively, using singlecycle kinetics fast runs without regeneration. Software-supported direct binding and inhibition assays enable measurement of active concentration. The precision and automation of the system generates highly reproducible data.


EMBL - European Molecular Biology Laboratory

Please Log in or Create an account to join the conversation. Due to these problems, it is difficult to perform a stable analysis of binding kinetics like KD. Index Recent Topics Search. Welcome, Guest.

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Biacore T200

Description: This Biacore T is a versatile system for high-quality characterization of molecular interactions, from ions to viruses. It is one platform that allows for comprehensive characterization of molecular interactions. The instrument also has reliable ligand-binding assays and has validated software to meet your regulatory expectations. There is confident selection and characterization of the smalled organic compounds to large multidomain proteins; fast, simple kinetic analysis. Description: The Biacore T is equipped with the most sensitive sensor that allows the study of interaction of even small compounds, such as small molecule inhibitors and peptides. The fully automated operation and independent temperature control for the detection chamber and sample chamber allows streamline and unattended operation for up to 4 days. Description: The Octet RED channel instrument provides analytical performance similar to the 8- channel Octet RED96 system, but with higher levels of throughput, speed, and flexibility.

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