Instrumentation

SEC-MALS provides simultaneous analysis of molar mass, size, and conformation of biomolecules, offering valuable insights into the assembly and stoichiometry of the samples being studied. This technique is particularly effective in detecting sample aggregation and identifying the different conformational populations present in the sample. It is commonly used in quality assessment of biomolecules to ensure consistency and uniformity across samples before more extensive characterization. When coupled with Dynamic Light Scattering (DLS), SEC-MALS allows for detailed resolution of size distributions within the biomolecular sample, further enhancing its analytical capabilities.

Differential Scanning Calorimetry or DSC is a powerful technique for measuring the thermal stability of biomolecules or their complexes, providing insights into conformational changes driven by the disruption of non-covalent interactions or rearrangements in tertiary structure. The MicroCal PEAQ DSC is particularly effective for quantitatively characterizing molecular stability and can be used to assess the impact of solvents on biomolecular structure, such as folding or unfolding processes. The technique identifies the melting temperature (Tm) of the analyzed samples, offering a clear indicator of their thermal stability.

Isothermal Titration Calorimetry or ITC is a highly sensitive, label-free technique that measures the thermodynamics and binding affinity between interacting molecules in solution. The Microcal PEAQ-ITC platform is specifically designed to study biomolecular associations, including both heteromolecular and homomolecular interactions. ITC is widely used for drug screening, evaluating the interaction between drugs and their respective targets. This technique measures heat exchange during molecular interactions, providing detailed insights into binding affinity and thermodynamic properties.

HPLC is an analytical technique used to separate and analyze organic mixtures composed of non-volatile, thermally unstable, and relatively large molecules. The JASCO HPLC system enables the separation of heterogeneous mixtures based on their retention times, making it suitable for a variety of samples, including both small molecules and biomolecules. This method is essential for achieving precise separations and analyses of complex samples in fields ranging from pharmaceuticals to biochemistry.

Real-time PCR or RT-PCR is a highly sensitive technique for detecting and quantifying gene expression levels. It is widely used for applications such as microarray validation, detection of pathogenic nucleic acids, and both relative and absolute analysis of target gene expression. The CFX96 Touch Real-Time PCR system, with its agile six-channel setup (five colors and one FRET channel), enables reliable detection of both singleplex and multiplex reactions. Its thermal gradient feature reduces optimization time for new samples, and it can also be utilized for protein samples, making it a versatile tool for genetic and protein analysis.

MALDI is a mass spectrometry technique where samples are ionized into charged molecules, and the mass-to-charge (m/z) ratio is measured. In the Bruker Daltonics MALDI-TOF mass spectrometer, the ion source is matrix-assisted laser desorption/ionization (MALDI), while the mass analyzer is a time-of-flight (TOF) analyzer. This technique is particularly effective for analyzing biomolecules, including DNA, proteins, peptides, and carbohydrates, as well as various organic molecules like polymers and dendrimers. Unlike traditional ionization methods, MALDI minimizes fragmentation and damage to fragile macromolecules, making it ideal for analyzing large, complex molecules.

The N-term Protein Sequencer is a specialized tool for determining the amino acid sequence of proteins from the N-terminal end. By accurately sequencing peptides, it provides essential insights into protein structure and function. This method is critical in proteomics for understanding protein modifications, identifying post-translational changes, and verifying protein identity. The sequencer is an essential instrument for researchers studying protein function and interactions in various biological systems.

The Biacore T200 is a high-performance system designed for real-time, label-free biomolecular interaction analysis using surface plasmon resonance (SPR). This technique measures the interaction between an immobilized partner molecule on the sensor chip and a flowing analyte through a microfluidic system. The SPR response is based on changes in the refractive index near the sensor surface, providing valuable information about the binding kinetics, affinity, and concentration of the interacting biomolecules. It is widely used in drug development, biomolecular research, and the study of protein-protein, protein-DNA, and protein-ligand interactions.

The HORIBA/FluoroMax-4 is a high-end fluorescence spectrophotometer used to analyze the fluorescence emitted by molecules based on their unique fluorescent properties. Fluorescence occurs when a molecule absorbs photons, which excites its electrons to a higher energy state. Fluorescence spectroscopy employs a light beam to excite these molecules, causing them to emit light. This emitted light is then directed through a filter and onto a detector for analysis, enabling the identification of molecules or changes in molecular structure. This technique is widely used in research to study molecular interactions, protein folding, and chemical reactions.

The Akta Pure system offers cutting-edge Fast Protein Liquid Chromatography or FPLC solutions for purifying protein samples, enabling users to obtain purified samples ranging from micrograms to milligrams. With a variety of gel filtration options, the system supports sample purification through Size Exclusion and Ion Exchange methods. Compatible with tag-specific columns, the Akta Pure system is highly customizable to meet the unique requirements of each purification process, making it an essential tool for researchers focused on high-efficiency protein separation and analysis.

The Circular Dichroism (CD) spectrometer is a specialized absorbance spectrophotometer that measures the difference in absorbance of right- and left-circularly polarized light by a substance. This technique is particularly useful for analyzing the secondary and tertiary structures of chiral molecules or chromophores, as well as studying structural changes caused by temperature variations or denaturing agents. With temperature-dependent CD and stock flow capabilities, the J-1500 offers valuable insights into protein folding, conformational changes, and stability under various conditions.

The Fourier Transform Infrared (FTIR) spectrometer, equipped with a fast recovery TSG detector and Jasco FT/IR-4700 data station, provides precise infrared absorption spectra for identifying both organic and inorganic compounds in a sample. By analyzing the absorption frequencies in the range of 600–4000 cm−1, FTIR enables the detection of specific molecular groups within the sample. The data obtained is processed through automated software, offering a detailed spectrum that reveals the chemical composition and structural features of the sample, making it a powerful tool for material identification and analysis.