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Biosensors

Biosensors are analytical devices that combine a biological component with a physicochemical detector to detect and quantify specific substances.
These innovative tools leverage biological recognition elements, such as enzymes, antibodies, or nucleic acids, to identify and measure target analytes with high specificity and sensitivity.
Biosensors have a wide range of applications in medical diagnostisc, environmental monitoring, and industrial process control, enabling rapid, cost-effective, and accurate analysis.
By integrating cutting-edge sensing technologies with advanced data analysis, biosensors are revolutionizing research and advancing our understanding of complex biological systems.
Discover the latest developments and optimize your biosensors research with AI-powered platforms that enhance reproducibility and accuracy.

Most cited protocols related to «Biosensors»

1
Simultaneous Biosensor Imaging and PA-Rac Activation
Imaging experiments were conducted on an Olympus FluoView 1000 laser scanning confocal microscope and an Olympus IX81-ZDC inverted microscope. Biosensor imaging was performed as previously described8 (link),29 . Simultaneous biosensor imaging and activation of PA-Rac was achieved using a MAG Biosystems FRAP-3D add-on (Photometrics) for galvanometer control of laser position. Detailed materials and methods are included in the supplementary information.
Wu Y.I., Frey D., Lungu O.I., Jaehrig A., Schlichting I., Kuhlman B, & Hahn K.M. (2009). A genetically-encoded photoactivatable Rac controls the motility of living cells. Nature, 461(7260), 104-108.
Publication 2009
Biosensors Microscopy Microscopy, Confocal
2
Simultaneous Biosensor Imaging and PA-Rac Activation
Imaging experiments were conducted on an Olympus FluoView 1000 laser scanning confocal microscope and an Olympus IX81-ZDC inverted microscope. Biosensor imaging was performed as previously described8 (link),29 . Simultaneous biosensor imaging and activation of PA-Rac was achieved using a MAG Biosystems FRAP-3D add-on (Photometrics) for galvanometer control of laser position. Detailed materials and methods are included in the supplementary information.
Wu Y.I., Frey D., Lungu O.I., Jaehrig A., Schlichting I., Kuhlman B, & Hahn K.M. (2009). A genetically-encoded photoactivatable Rac controls the motility of living cells. Nature, 461(7260), 104-108.
Publication 2009
Biosensors Microscopy Microscopy, Confocal
3
Quantifying Spatial-Temporal Coupling of Cellular Dynamics
Corrected biosensor images were segmented and cell edge displacements tracked as in13 (link). Sampling windows of 0.9 μm depth and 1.8 - 3μm width were constructed to follow morphological changes at a fixed distance from the cell edge. For each window, biosensor activation time courses were recorded. For windows placed at the cell edge, a time course of protrusion/retraction velocity was recorded additionally. Coupling of two activity time courses was analyzed per window by Pearson's cross-correlation function. Subsequently, for a cell the per-window correlation functions were averaged over all windows following the edge at a specific distance D (Fig. 1i). Per-cell correlation functions were averaged over multiple cells and statistically analyzed by bootstrap sampling to determine the significance and time lag of the coupling between two activities. All procedures are detailed in Supplementary Methods.
Machacek M., Hodgson L., Welch C., Elliott H., Pertz O., Nalbant P., Abell A., Johnson G.L., Hahn K.M, & Danuser G. (2009). Coordination of Rho GTPase activities during cell protrusion. Nature, 461(7260), 99-103.
Publication 2009
Biosensors Cells Displacement, Psychology Physiology, Cell Place Cells
4
FRET Biosensor Assay in HeLa and Cos7 Cells
HeLa cells were purchased from the Human Science Research Resources Bank (Sennanshi, Japan). The Cos7 cells used were Cos7/E3, a subclone of Cos7 cells established by Y. Fukui (National Research Institute of Health, Taiwan, Republic of China). HeLa cells and Cos7 cells were maintained in DMEM (Sigma-Aldrich, St. Louis, MO) supplemented with 10% FBS. The cells were plated on 35-mm glass base dishes or 96-well glass base plates (Asahi Techno Glass, Tokyo, Japan), which were coated with collagen type I (Nitta Gelatin, Osaka, Japan). Plasmids encoding FRET biosensors were transfected into HeLa cells and Cos7 cells by 293fectin or Lipofectamine 2000, according to the manufacturer's instructions (Invitrogen, San Diego, CA), respectively. EGF was purchased from Sigma-Aldrich. dbcAMP, TPA, Calyculin A, Anisomycin, PD153035, and JNK inhibitor VIII were purchased from Calbiochem (La Jolla, CA). PD184352 was obtained from Toronto Research Chemicals (Ontario, Canada). BI-D1870 was purchased from Symansis (Shanghai, China). Rapamycin was obtained from LC Laboratories (Woburn, MA). PLX-4720 was purchased from Selleck Chemicals (Houston, TX). The expression vector of piggyBac transposase was provided by A. Bradley (Wellcome Trust Sanger Institute, Cambridge, UK; Yusa et al., 2009 (link)). Phos-tag was obtained from the Phos-tag Consortium (Hiroshima, Japan; www.phos-tag.com). Anti-green fluorescence protein (GFP) sera were prepared in our laboratory. LI-COR (Lincoln, NE) blocking buffer and the IRDye680- and IRDye800-conjugated anti–rabbit and anti–mouse immunoglobulin G secondary antibodies were obtained from LI-COR.
Komatsu N., Aoki K., Yamada M., Yukinaga H., Fujita Y., Kamioka Y, & Matsuda M. (2011). Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular Biology of the Cell, 22(23), 4647-4656.
Publication 2011
1,3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol Anisomycin Anti-Antibodies BI D1870 Biosensors Bucladesine Buffers calyculin A Cells Cloning Vectors Collagen Type I Fluorescence Resonance Energy Transfer Gelatins Green Fluorescent Proteins HeLa Cells Hyperostosis, Diffuse Idiopathic Skeletal Immunoglobulin G IRDye800 lipofectamine 2000 Manpower Mus PD 153035 PD 184352 Plasmids PLX 4720 Rabbits Serum Sirolimus Transposase
5
FRET Microscopy Imaging Protocol
FRET images were obtained and processed using essentially the same conditions and procedures as previously reported (Aoki and Matsuda, 2009 (link)). Briefly, HeLa cells or Cos7 cells expressing FRET biosensors were starved for 6–12 h with phenol red–free DMEM/F12 medium or Medium 199 (Invitrogen) containing 0.1% bovine serum albumin (BSA) or phenol red–free M199 (Invitrogen) with 20 mM HEPES and 0.1% BSA. Starved cells were treated with stimulus, followed by the addition of inhibitors if necessary. Cells were imaged with an inverted microscope (IX71 or IX81; Olympus, Tokyo, Japan) equipped with a 60× objective lens (Olympus), a cooled CCD camera (CoolSNAP HQ or CoolSNAP K4; Roper Scientific, Tucson, AZ), an LED illumination system (CoolLED precisExcite; Molecular Devices, Sunnyvale, CA), an IX2-ZDC laser-based autofocusing system (Olympus), and an MD-XY30100T-Meta automatically programmable XY stage (SIGMA KOKI, Tokyo, Japan). The following filters used for the dual-emission imaging studies were obtained from Omega Optical (Brattleboro, VT): an XF1071 (440AF21) excitation filter, an XF2034 (455DRLP) dichroic mirror, and two emission filters (XF3075 for CFP and XF3079 for YFP). After background subtraction, FRET/CFP ratio images were created with MetaMorph software (Universal Imaging, West Chester, PA), and represented by the intensity-modulated display mode. In the intensity-modulated display mode, eight colors from red to blue are used to represent the FRET/CFP ratio, with the intensity of each color indicating the mean intensity of FRET and CFP. For the quantification, the FRET and CFP intensities were averaged over the whole cell area, and the results were exported to Excel software (Microsoft Corporation, Redmond, WA). In some experiments, the FRET/CFP value from before 10 min to the time of stimulation was averaged and used as the reference. The ratio of raw FRET/CFP value versus the reference value was defined as the normalized FRET/CFP value.
Komatsu N., Aoki K., Yamada M., Yukinaga H., Fujita Y., Kamioka Y, & Matsuda M. (2011). Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular Biology of the Cell, 22(23), 4647-4656.
Publication 2011
Biosensors Cells Fluorescence Resonance Energy Transfer HeLa Cells HEPES inhibitors Lens, Crystalline Light Medical Devices Microscopy Serum Albumin, Bovine Vision

Most recents protocols related to «Biosensors»

1
Synthetic Urine-based Electrochemical Biosensor for Urine Albumin Detection
Not available on PMC !

Example 7

Synthetic urine is prepared by dissolving 14.1 g of NaCl, 2.8 g KCl, 17.3 g of urea, 19 ml ammonia water (25%), 0.60 g CaCl2 and 0.43 g MgSO4 in 0.02 mole/L of HCl. The final pH of synthetic urine is adjusted to 6.04 by using HCl and ammonia water.

40 mg Sigma creatinine is dissolved in 10 ml of synthetic urine solution. 3 mg of human albumin is dissolved in 10 ml of synthetic urine solution to prepare the micro albumin solution.

4 mg Sigma hemin is dissolved in 20 ml of synthetic urine, 20 μL Hemin solution is used as a receptor for urine albumin detection at different creatinine concentration.

A desired volume of the biological sample (synthetic urine) is taken and dispensed on the electrode of the biosensor device and the corresponding cyclic voltammogram is obtained by the CHI-Electrochemical workstation using the potential window, that varies from 0 V to −1 V with scan rate of 0.1 V/sec.

The albumin content in the urine sample binds hemin thereby demonstrates a linear decrease in peak redox current with urine albumin concentration as shown in FIG. 15(a) for different creatinine concentrations. If the concentration of albumin in urine sample is increased, then the albumin increasingly binds with hemin thereby reducing the free hemin concentration on the electrode resulting in the decrease in peak redox current of free hemin. FIG. 16 shows the urine albumin concentrations, urine creatinine concentrations and calculated ACR for different samples.

The values of concentrations of the urine albumin (mg/L) and creatinine for different samples is shown in Table 4.

TABLE 4
SampleUrine albuminUrine CreatinineACR
Number(mg/L)(mg/dL)(mg/g)
1526.719
22026.775
35026.7187
410026.7375
515026.7562
65133.34
720133.315
850133.338
9100133.375
10150133.3113

US11867654B2. Device and method for detecting creatinine and albumin to creatinine ratio (2024-01-09). INDIAN INSTITUTE OF SCIENCE [IN]. Inventors: Vinay Kumar [IN], Navakanta Bhat [IN], Nikhila Kashyap Dhanvantari Madhuresh [IN].
Full text: Click here
Patent 2024
Albumins Ammonium Hydroxide Biopharmaceuticals Biosensors Creatinine Hemin Moles Oxidation-Reduction Radionuclide Imaging Receptors, Albumin Serum Albumin, Human Sodium Chloride Sulfate, Magnesium Urea Urine
2
Thin-Film Electrode Characterization
Not available on PMC !

Example 12

Different thin-film electrodes were tested using the Type 1 Linear Sweep Voltammetry Test. In more detail, thin-film electrodes formed with a stainless steel 304 (SS304) conductive layer, including an electrode with an amorphous carbon layer deposited thereon in a pure Ar atmosphere, an electrode with an amorphous carbon-containing layer deposited thereon in a 20% nitrogen atmosphere, and an electrode with an amorphous carbon-containing layer deposited thereon in a 50% nitrogen atmosphere were tested. The electrodes were all produced in a roll-to-roll sputter coater.

Anodic polarization scans in PBS, with 1 mM K4[FeII(CN)6] redox mediator added, at 25 mV/s using a saturated calomel (SCE) reference electrode and each of the SS304 electrodes as the working electrode. The results are illustrated graphically in FIG. 11. A review of FIG. 11 reveals that the electron transfer kinetics between the mediator and electrode are slightly faster when the carbon layer is sputtered in a pure Ar atmosphere, compared to a N2 containing atmosphere. However, even the films sputtered in a 1:1 Ar:N2 gas mixture is still useful in a biosensor and has an increase in deposition rate of ˜164% compared to carbon sputtered in pure Ar.

US11881549B2. Physical vapor deposited electrode for electrochemical sensors (2024-01-23). EASTMAN CHEMICAL COMPANY [US]. Inventors: Dennis Lee Ashford, II [US], Daniel Patrick Puzzo [US], Spencer Erich Hochstetler [US].
Full text: Click here
Patent 2024
Atmosphere Biosensors calomel Carbon Electric Conductivity Electron Transport Kinetics Nitrogen Oxidation-Reduction Radionuclide Imaging Stainless Steel
3
Antibody Competition Assay on CD25
Not available on PMC !

Example 5

Antibody competitions were performed on a Forte Bio Octet Red96 system (Pall Forte Bio Corp., USA) using a standard sequential binding assay. 26.8 nM recombinant human CD25his tagged was loaded onto Ni-NTA Biosensors for 200 s. After base line step on kinetic buffer sensors were exposed to 66.6 nM of first antibody for 600 s followed by a second anti-CD25 antibody (also at 66.6 nM for 600 s). Data was processed using Forte Bio Data Analysis Software 9.0. Additional binding by a second antibody indicates an unoccupied epitope (no competition for the epitope), while no binding indicates epitope blocking (competition for the epitope). The results are shown in in FIG. 5.

US11873341B2. Anti-CD25 for tumour specific cell depletion (2024-01-16). Tusk Therapeutics Ltd. [GB], Cancer Research Technology Limited [GB]. Inventors: Anne Goubier [GB], Beatriz Goyenechea Corzo [GB], Josephine Salimu [GB], Kevin Moulder [GB], Pascal Merchiers [GB], Sergio Quezada [GB].
Full text: Click here
Patent 2024
Antibodies, Anti-Idiotypic BaseLine dental cement Biological Assay Biosensors Buffers Epitopes Homo sapiens IL2RA protein, human Immunoglobulins Kinetics
4
Antibody Competition Assay for CD25 Epitope Mapping
Not available on PMC !

Example 8

Antibody competitions were performed on a Forte Bio Octet® Red96 system (Pall Forte Bio Corp., USA) using a standard sequential binding assay. 26.8 nM recombinant human CD25his tagged was loaded onto Ni-NTA Biosensors for 200s. After base line step on kinetic buffer sensors were exposed to 66.6 nM of first antibody for either 600s or 1800s followed by a second anti-CD25 antibody (also at 66.6 nM for either 600s or 1800s). Data was processed using Forte Bio Data Analysis Software 9.0. Additional binding by a second antibody indicates an unoccupied epitope (no competition for the epitope), while no binding indicates epitope blocking (competition for the epitope).

Results

Non blockers of IL-2 signal mAbs (Antibody 1 and Antibody 3) compete with each other or with 7G7B6 and MA251 while they do not compete with research Daclizumab or research Basiliximab (examples (A) to (N), FIG. 24). IL-2 signalling blockers (i.e. TSK031) do compete with the research Daclizumab and research Basiliximab and do not compete with 7G7B6 (examples (O) to (Q), FIG. 24).

US11879014B2. Method of treating cancer or depleting regulatory T cells in a subject by administering a human IGG1 anti-CD25 antibody (2024-01-23). Tusk Therapeutics Ltd. [GB], Cancer Research Technology Limited [GB]. Inventors: Anne Goubier [GB], Josephine Salimu [GB], Kevin Moulder [GB], Beatriz Goyenechea Corzo [GB], Pascal Merchiers [GB], Sergio Quezada [GB], Karl Peggs [GB], Frederick Arce Vargas [GB], Isabelle Solomon [GB].
Full text: Click here
Patent 2024
Antibodies, Anti-Idiotypic BaseLine dental cement Basiliximab Biological Assay Biosensors Buffers Daclizumab Epitopes Homo sapiens IL2RA protein, human Immunoglobulins Kinetics Monoclonal Antibodies
5
Binding Affinities of VEGF-C and VEGF-D
Not available on PMC !

Example 4

The binding of VEGF-C and VEGF-D to VGX-300 or VGX-301-ΔN2 was analyzed by surface plasmon resonance (SPR) performed using the PrateOn XPR36 biosensor (Bio-Rad). Either VGX-300 or VGX-301-ΔN2 was captured onto protein G′ immobilized onto a GLM sensor chip and the affinity of the molecule to VEGF-C or VEGF-D was measured. The results of the affinity experiment are provided below in Table 5.

TABLE 5
ka(M−1s−1) × 106 kd(s−1) × 10−5 KD(pM)
Human VEGF-C
VGX-300 2.18 ± 0.05 1.11 ± 0.12  5.1 ± 0.6
VGX-301-ΔN2 2.79 ± 0.04 1.03 ± 0.08  3.7 ± 0.3
Human VEGF-D
VGX-300 4.9 ± 0.1 3.23 ± 0.16 625 ± 21
VGX-301-ΔN2 5.7 ± 0.1 3.88 ± 0.03 677 ± 12

The data presented in Table 5 above shows that the VGX-300 and VGX-301-ΔN2 samples bound human VEGF-C and VEGF-D with near identical affinities, with both molecules showing stronger binding to VEGF-C than VEGF-D.

US11866739B2. Ligand binding molecules and uses thereof (2024-01-09). VEGENICS PTY LIMITED [AU]. Inventors: Michael Gerometta [AU], Timothy Adams [AU].
Full text: Click here
Patent 2024
Biosensors DNA Chips G-substrate Homo sapiens Surface Plasmon Resonance Vascular Endothelial Growth Factor C Vascular Endothelial Growth Factor D

Top products related to «Biosensors»

1
Octet red96 by Molecular Devices
Sourced in United States, Germany
The Octet RED96 is an analytical instrument designed for label-free, real-time monitoring of biomolecular interactions. It utilizes biolayer interferometry technology to measure association and dissociation kinetics, affinity, and concentration of molecules in solution.
2
Octet red96 system by Molecular Devices
Sourced in United States, United Kingdom
The Octet RED96 system is a label-free, real-time, and high-throughput biomolecular interaction analysis instrument. It utilizes biolayer interferometry technology to measure the association and dissociation of biomolecules in solution, providing quantitative kinetic and affinity data.
3
Streptavidin biosensor by Molecular Devices
Sourced in United States, China
Streptavidin biosensors are analytical devices used to detect and measure the presence of specific biomolecules in samples. They function by utilizing the high-affinity binding interaction between streptavidin and biotin, a commonly used labeling molecule. These biosensors enable the sensitive and selective detection of target analytes in various research and diagnostic applications.
4
Blitz system by Molecular Devices
Sourced in United States, Spain
The BLItz system is a label-free, real-time molecular interaction analysis instrument that measures binding kinetics and affinity. It utilizes biolayer interferometry (BLI) technology to monitor biomolecular interactions in real-time without the need for labeling. The BLItz system provides a compact and versatile solution for a wide range of applications, including protein-protein, protein-small molecule, and protein-nucleic acid interactions.
5
Octet red by Molecular Devices
Sourced in United States, United Kingdom
The Octet Red is a label-free, real-time interaction analysis system that measures biomolecular interactions. It utilizes biolayer interferometry technology to monitor the association and dissociation of analytes in a sample. The Octet Red is designed to provide quantitative kinetic and affinity data for a wide range of biomolecular interactions.
6
Octet red96 instrument by Molecular Devices
Sourced in United States, Germany
The Octet RED96 instrument is a label-free, real-time analysis system used for biomolecular interaction studies. It measures binding kinetics and affinity between a wide range of molecules, including proteins, peptides, small molecules, and nucleic acids. The instrument utilizes Bio-Layer Interferometry (BLI) technology to monitor the interaction of biomolecules in real-time.
7
Octet red384 by Molecular Devices
Sourced in United States
The Octet RED384 is a high-throughput label-free detection system for biomolecular interaction analysis. It is capable of simultaneously monitoring up to 384 samples in real-time, providing efficient and accurate data collection for a wide range of applications.
8
Ni nta biosensor by Molecular Devices
Sourced in United States
Ni-NTA biosensors are a type of lab equipment used for the detection and analysis of biomolecular interactions. They utilize the high-affinity binding between nickel-nitrilotriacetic acid (Ni-NTA) and polyhistidine-tagged proteins to facilitate the capture and monitoring of target analytes in real-time.
9
Biacore t200 by GE Healthcare
Sourced in United States, Sweden, United Kingdom, Australia, Germany, Georgia, France, Japan, New Zealand
The Biacore T200 is a label-free, real-time interaction analysis system designed for studying molecular interactions. It provides quantitative data on binding kinetics, affinity, and specificity between molecules. The system utilizes surface plasmon resonance (SPR) technology to detect and measure these interactions without the need for labeling.
10
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

More about "Biosensors"

Biosensors are innovative analytical tools that combine biological components, such as enzymes, antibodies, or nucleic acids, with physicochemical detectors to identify and measure specific substances with high precision and sensitivity.
These cutting-edge devices have a wide range of applications in medical diagnostics, environmental monitoring, and industrial process control, enabling rapid, cost-effective, and accurate analysis.
Leveraging advanced sensing technologies and data analysis, biosensors are revolutionizing research and our understanding of complex biological systems.
From the Octet RED96 system and Streptavidin biosensors to the BLItz system and Ni-NTA biosensors, these instruments offer powerful capabilities for biomolecular interaction analysis, protein quantification, and more.
The Octet RED and Octet RED384 instruments, for example, utilize biolayer interferometry (BLI) to provide real-time, label-free measurements of biomolecular interactions.
Similarly, the Biacore T200 system employs surface plasmon resonance (SPR) technology to study a wide range of analyte-ligand interactions.
By integrating these cutting-edge biosensor platforms with AI-powered optimization and analysis tools, like those offered by PubCompare.ai, researchers can enhance the reproducibility and accuracy of their biosensors research.
This allows for the rapid identification of the best protocols and products, streamlining the development of innovative solutions for medical, environmental, and industrial applications.
Unlock the full potential of biosensors research and discover the latest advancements in this rapidly evolving field.
Leverage the power of AI-driven platforms, such as PubCompare.ai, to optimize your workflows and advance your understanding of complex biological systems.