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Surface-Active Agents

Surface-Active Agents, also known as surfactants, are compounds that lower the surface tension of a liquid, allowing easier spreading and penetration.
They are widely used in a variety of industrial and consumer applications, including detergents, emulsifiers, wetting agents, and dispersants.
Surface-Active Agents can be derived from natural sources, such as plant oils or animal fats, or synthetically produced.
These versatile compounds play a crucial role in enhancing the effectiveness and efficiency of many products and processes.
Researchers can optimize their Surface-Active Agent research using PubCompare.ai, a leading AI-driven platform that helps identify the best protocols and products from literature, preprints, and patents, while improving reproducibility and accuracy.

Most cited protocols related to «Surface-Active Agents»

In single-cell RNA-Seq, small amounts of sample loss during a number of steps can lead to significant decreases in transcript detection sensitivity. A decrease in assay sensitivity results in data that is only accurate and reproducible for highly expressed genes, limiting the scope and confidence of gene expression analyses. Further complications in assay sensitivity arise from an uneven distribution of sequencing reads along a transcript; usually, in SMARTer, there is a bias towards more reads at the 3′ end of the transcript. Even coverage along a transcript improves the accuracy of analytical tools used to quantify gene expression and transcript isoform abundance. A method published by Picelli et al (Nature Methods, 2013) modified the traditional SMARTer protocol to address this by improving transcript detection, coverage, accuracy, yield, and cost. Following the same strategy as SMARTer library construction, Smart-seq2 uses several alternative reagents to generate whole-transcriptome full-length cDNA libraries.
Avoiding small-volume, bead-based SPRI cleanups of each sample is an effective way of reducing loss and increasing assay sensitivity. Lysing single cells in a guanidine thiocyanate buffer necessitates SPRI cleanup due to the protein denaturing effects of the compound, which will affect downstream reactions, like reverse transcription. Multiple alternative lysis buffers exist that address this. The Ambion Single Cell Lysis buffer (Life technologies, #4458235), often used for single-cell RT-PCR, only requires the addition of a stop solution to inactivate its lytic activity before subsequent reactions. A hypotonic lysis buffer with small amounts of RNase-inhibitor and surfactant, as described in Smart-seq2, is the preferred buffer due to the lack of a need for a post-lysis cleanup or the addition of a stop solution prior to reverse transcription. However, the optimal lysis strategy will depend on the experimental system being analyzed.
Smart-seq2 takes additional steps to minimize sample loss during library construction. The reverse transcription is improved by the addition of betaine and additional magnesium chloride to the reaction mix and by the use of a template-switch oligonucleotide with one locked nucleic acid (LNA) riboguanosine base. These improvements assist in the hybridization between the template-switch oligonucleotide and the cDNA product, thereby increasing the probability of successfully introducing a second PCR adapter onto the cDNA product (see Figure 1). A second key improvement was made in the preamplification PCR step, which can be heavily biased against either long transcripts or those containing regions with high G/C content. Picelli et al found that the preamplification PCR is improved by using the KAPA HiFi HotStart ReadyMix, which dramatically improved coverage and sensitivity, particularly for GC-rich transcripts.
Publication 2014
Betaine Biological Assay Buffers cDNA Library Cells Crossbreeding DNA, Complementary Endoribonucleases Gene Expression Gene Expression Profiling Genes guanidine thiocyanate Hypersensitivity locked nucleic acid Magnesium Chloride Oligonucleotides Protein Isoforms Proteins Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription Single-Cell RNA-Seq Surface-Active Agents Transcriptome
- Grow healthy Arabidopsis plants until they are flowering (see Figure 1A).
Optional: Clip first bolts to encourage proliferation of many secondary bolts. Plants will be ready roughly 4–6 days after clipping. Optimal plants have many immature flower clusters and only few fertilized siliques, although a range of plant stages can be successfully transformed.
- Transform the DNA construct of interest into the appropriate Agrobacterium strain. Grow the transformed Agrobacterium on YEB (or LB) plates containing the appropriate antibiotics in a 28°C incubator.
- Select a colony and resuspend bacteria in 10 μl H2O. Plate half of the volume immediately as a lawn onto a YEB plate with the suitable antibiotics and incubate at 28°C for (2–3 days), and use the other half to verify the presence of your DNA construct by PCR analysis.
- Collect the densely grown bacteria from the plate by scraping, and resuspend them in 30 ml YEB in a sterile Falcon tube. The OD600 should be about 2.0.
- Per transformation prepare 120 ml of 5% sucrose solution containing 0.03% of Silwet L-77 (surfactant; Lehle Seeds), pour solution into a disposable plastic bag and add the bacteria.
- Dip the inflorescences of the plants into the Agrobacterium solution for 10 seconds, under gentle agitation. You should observe a film of liquid coating the plants. The bacteria are distributed to all plant parts including very young flower shoots by gently pressing the outside of the bag with your hands.
- Place dipped plants under a lid or cover for 16 to 24 hours to maintain high humidity (plants can be laid on their sides if necessary). Do not expose to excessive sunlight (the temperature under the lid can get high).
- Water and grow the plants as normal, tying up loose bolts with wax paper, tape, stakes, twist-ties, or by other means. Stop watering as seeds become mature.
- Harvest dry seeds.
- Select for transformants using appropriate antibiotics or herbicides.
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Publication 2006
Agrobacterium Antibiotics, Antitubercular Arabidopsis Bacteria Clip Herbicides Humidity Inflorescence Neoplasm Metastasis Plant Embryos Plants Recombinant DNA silwet L-77 Sterility, Reproductive Strains Sucrose Sunlight Surface-Active Agents

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Publication 2015
Anabolism Buffers Cells Centrifugation HFE-7500 Medical Devices Microchip Analytical Devices Surface-Active Agents Syringes
Three identical transcriptional cassettes for luxI, aiiA, and yemGFP were constructed by replacing a modular pZ plasmid’s promoter 47 (link) (with yemGFP) with the lux operon from the native Vibrio Fischeri operon (luxR up to luxI stop codon) 48 (link). LuxI and aiiA49 genes were cloned in place of yemGFP and a degradation tag was added to the carboxy-terminal of each. A previously used MG1655 strain of Escherichia coli1 was transformed with plasmids pTD103luxI/GFP(colE1,Kan) and pTD103aiiA(p15A,Amp) to create strain TDQS1 (Suppl. Info).
Each experiment started with a 1:1000 dilution of overnight culture grown in 50mL LB (10g/L NaCl) with antibiotics 100µg/ml ampicillin(Amp) and 50µg/ml kanamycin(Kan) for approximately 2 hours. Cells reached an OD600 of 0.05–0.1 and were spun down and concentrated in 5mL of fresh media with surfactant concentration of 0.075 Tween20 [Sigma-Aldrich, St.Louis,MO] before loading in a device.
Publication 2009
Aliivibrio fischeri Ampicillin Antibiotics, Antitubercular Cells Codon, Terminator Escherichia Genes Kanamycin Medical Devices Operon Plasmids Sodium Chloride Strains Surface-Active Agents Technique, Dilution Transcription, Genetic Tween 20
DNA samples were purchased from Sigma-Aldrich as desalted ss oligomers at 100 μM concentration in water. SPR measurements were recorded at 20°C with a Biacore T200 system (GE Healthcare). All experiments described herein were performed using ReDCaT with a single Sensor Chip SA (GE Healthcare), which has four flow cells each containing SA pre-immobilized to a carboxymethylated dextran matrix. Two types of protocol were followed (detailed in Supplementary Methods): ‘affinity’ protocols were used to determine the dissociation constants for specific protein–DNA interactions, and ‘screening’ protocols were used for all other types of experiment. For the screening experiments, flow cells 1 and 2 were used as the reference (FCref) and test flow cells (FCtest), respectively. For the affinity experiments, flow cells 3 and 4 were used as FCref and FCtest, respectively. Throughout the SPR procedures, all samples were prepared, and all experiments were performed, in HBS-EP+ buffer [150 mM NaCl, 3 mM EDTA, 0.05% (v/v) surfactant P20, 10 mM HEPES (pH 7.4); GE Healthcare]. A cartoon representation of the ReDCaT Chip methodology and a typical SPR sensorgram are shown in Figure 2.

The ReDCaT methodology. (A) Procedure for creating, using and regenerating the ReDCaT Chip, specifically illustrating the events taking place in the test flow cell. (B) A typical sensorgram for the test flow cell of the ReDCaT Chip showing the responses observed during its use and regeneration. The response returns to the original baseline after stripping off the test DNA. (C) The composition of bound DNA in the reference and test flow cells before injecting protein in the ReDCaT screening and affinity experiments. (D) Key to the macromolecular components illustrated in the other three panels.

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Publication 2013
B-Lymphocytes Buffers Cells Dextran DNA Chips Edetic Acid HEPES HSP40 Heat-Shock Proteins Place Cells Proteins PTPRC protein, human Regeneration Sodium Chloride Surface-Active Agents

Most recents protocols related to «Surface-Active Agents»

Example 5

Three sets of samples were prepared with polyamide 12 from RTP. 10,000 cSt PDMS, 23 wt % polyamide 12 relative to the weight of PDMS and polyamide combined, 1 wt % AEROSIL® R812S silica nanoparticles relative to the weight of the polyamide, and optionally surfactant (wt % relative to the weight of the polyamide) were placed in a glass kettle reactor. The headspace was purged with argon and the reactor was maintained under positive argon pressure. The components were heated to over 220° C. over about 60 minutes with 300 rpm stirring. At temperature, the rpm was increased to 1250 rpm. The process was stopped after 90 minutes and allowed to cool to room temperature while stirring. The resultant mixture was filtered and washed with heptane. A portion of the resultant particles was screened (scr) through a 150-μm sieve. Table 3 includes the additional components of the mixture and properties of the resultant particles.

TABLE 3
Max
ReactorScreened Particle SizeNot Screened Particle Size
Temp.(μm or unitless)(μm or unitless)
SampleSurfactant(° C.)D10D50D90SpanD10D50D90Span
5-1none22316.737.477.31.6216.938.71222.72
5-22.5%22644.267.71050.9041.468.11311.32
CALFAX ®
DB-45
5-31%22619.243.395.81.7719.448.82073.84
docusate
sodium

FIGS. 16 and 17 are the volume density particle size distribution for the particles screened and not screened, respectively.

This example illustrates that the inclusion of surfactant and the composition of said surfactant can be another tool used to tailor the particle characteristics.

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Patent 2024
Aerosil Argon DB 19 Docusate Sodium Figs Heptane nylon 12 Nylons Pressure Silicon Dioxide Surface-Active Agents

EXAMPLE 1

In an AISI 316 steel vertical autoclave, equipped with baffles and a stirrer working at 570 rpm, 3.5 liter of demineralized water were introduced. The temperature was then brought to reaction temperature of 80° C. and the selected amount of 34% w/w aqueous solution of cyclic surfactant of formula (VI) as defined above, with Xa=NH4, was added. VDF and ethane were introduced to the selected pressure variation reported in Table 1. A gaseous mixture of TFE-VDF in the molar nominal ratio reported in Table 1 was subsequently added via a compressor until reaching a pressure of 20 bar. Then, the selected amount of a 3% by weight water solution of sodium persulfate (NaPS) as initiator was fed. The polymerization pressure was maintained constant by feeding the above mentioned TFE-VDF while adding the PPVE monomer at regular intervals until reaching the total amount indicated in the table 1.

When 1000 g of the mixture were fed, the reactor was cooled at room temperature, the latex was discharged, frozen for 48 hours and, once unfrozen, the coagulated polymer was washed with demineralized water and dried at 160° C. for 24 hours.

The composition of the obtained polymer F-1, as measured by NMR, was Polymer (F-1)(693/99): TFE (69.6% mol)—VDF (27.3% mol)—PPVE (2.1% mol), having melting point Tm=218° C. and MFI=5 g/10′.

The procedure of example 1 was repeated, by introducing the amount of ingredients indicated in the third column of Table 1.

The composition of the obtained polymer P-1, as measured by NMR, was Polymer (C-1)(693/67): TFE (71% mol)—VDF (28.5% mol)—PPVE (0.5% mol), having melting point Tm=249° C. and MFI=5 g/10′.

EXAMPLE 2

The procedure of example 1 was repeated, by introducing the amount of ingredients indicated in the second column of Table 1.

The composition of the obtained polymer F-2, as measured by NMR, was Polymer (F-1)(693/100): TFE (68% mol)—VDF (29.8% mol)—PPVE (2.2% mol), having melting point Tm=219° C. and MFI=1.5 g/10′.

In an AISI 316 steel horizontal reactor, equipped with a stirrer working at 42 rpm, 56 liter of demineralized water were introduced. The temperature was then brought to reaction temperature of 65° C. and the selected amount of 40% w/w aqueous solution of cyclic surfactant of formula (VI) as defined above, with X1=NH4, was added. VDF and ethane were introduced to the selected pressure variation reported in Table 1.

A gaseous mixture of TFE-VDF in the molar nominal ratio reported in Table 1 was subsequently added via a compressor until reaching a pressure of 20 bar.

Then, the selected amount of a 0.25% by weight water solution of sodium persulfate (NaPS) as initiator was fed. The polymerization pressure was maintained constant by feeding the above mentioned TFE-VDF while adding the PPVE monomer at regular intervals until reaching the total amount indicated in the table 1.

When 16000 g of the mixture were fed, the reactor was cooled at room temperature, the latex was discharged, frozen for 48 hours and, once unfrozen, the coagulated polymer was washed with demineralized water and dried at 160° C. for 24 hours. The composition of the obtained polymer C-2, as measured by NMR, was Polymer (C-2)(SA1100): TFE (70.4% mol)—VDF (29.2% mol)—PPVE (0.4% mol), having melting point Tm=232° C. and MFI=8 g/10′.

EXAMPLE 3

The procedure of Comparative Example 2 was repeated, by introducing the following changes:

    • demineralized water introduced into the reactor: 66 litres;
    • polymerization temperature of 80° C.
    • polymerization pressure: 12 abs bar
    • Initiator solution concentration of 6% by weight
    • MVE introduced in the amount indicated in table 1
    • Overall amount of monomers mixture fed in the reactor: 10 000 g, with molar ratio TFE/VDF as indicated in Table 1.

All the amount of ingredients are indicated in the fifth column of Table 1.

The composition of the obtained polymer (C-3), as measured by NMR, was Polymer (C-3)(693/22): TFE (72.1% mol)—VDF (26% mol)—PMVE (1.9% mol), having melting point Tm=226° C. and MFI=8 g/10′.

TABLE 1
(F-1)(F-2)(C-1)(C-2)(C-3)
Surfactant solution [g]505050740800
Surfactant [g/l]4.854.854.855.284.12
Initiator solution [ml]1001001002500600
Initiator [g/kg]3.03.03.00.396.0
VDF [bar]1.81.801.81.8
TFE/VDF mixture 70/3070/3070/3070/3069/301
[molar ratio]
FPVE [g]1221223166002
Ethane [bar]0.60.30.2520.1
1gaseous mixture containing 1% moles of perfluoromethylvinylether (FMVE);
2initial partial pressure of FMVE 0.35 bar.

The results regarding polymers (F-1), (F-2) of the invention, and comparative (C-1), (C-2) and (C-3) are set forth in Table 2 here below

TABLE 2
693/99693/100693/67SA1100693/14
(F-1)(F-2)(C-1)(C-2)(C-3)
Elongation at5777392904035
break [%, 200° C.]
Tensile modulus425374484594500
[MPa, 23° C.]
Tensile yield stress11.611.414.015.512.5
[MPa, 23° C.]
Tensile modulus29385676
[MPa, 170° C.]
Tensile modulus1210484723
[MPa, 200° C.]
SHI [MPa, 23° C.]3.65.11.91.61.7
ESR as yieldingNoNoYieldingYieldingYielding
[time, 23° C.]YieldingYieldingafter 1after 1after 1
minminmin

In particular, the polymer (F) of the present invention as notably represented by the polymers (F-1), (F-2), surprisingly exhibits a higher elongation at break at 200° C. as compared to the polymers (C-1) and (C-2) of the prior art.

Also, the polymer (F) of the present invention as notably represented by the polymers (F-1), (F-2), despite its lower tensile modulus, which remains nevertheless in a range perfectly acceptable for various fields of use, surprisingly exhibits a higher strain hardening rate by plastic deformation as compared to the polymers (C-1) and (C-2) of the prior art.

Finally, the polymer (F) of the present invention as notably represented by the polymers (F-1) and (F-2) surprisingly exhibits higher environmental stress resistance when immersed in fuels as compared to the polymers (C-1) and (C-2) of the prior art.

Yet, comparison of polymer (F) according to the present invention with performances of polymer (C-3) comprising perfluoromethylvinylether (FMVE) as modifying monomer shows the criticality of selecting perfluoropropylvinylether: indeed, FMVE is shown producing at similar monomer amounts, copolymer possessing too high stiffness, and hence low elongation at break, unsuitable for being used e.g. in O&G applications.

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Patent 2024
Ethane Fluorocarbon Polymers Freezing G-800 Gases Latex Molar N-(4-aminophenethyl)spiroperidol Nevus Partial Pressure Polymerization Polymers Pressure Sclerosis sodium persulfate Steel Surface-Active Agents

Example 7

Table 7 showed an improved stability of the disinfectant formulations upon including ethanol as a stabilizing agent in the formulations, wherein the disinfectant formulations comprised a mixture of lactic acid and formic acid as the C1-8 organic acids, and sodium sarcosinate as the amino acid based surfactant. Formulation Q, which did not include any ethanol stabilizing agent, was an unstable cloudy solution that resulted in a phase separation. Upon including ethanol stabilizing agent in the formulations (Formulations R and S), the stable clear solutions were achieved.

TABLE 7
FormulationQRS
IngredientsOn 100%On 100%On 100%
SLES 2EO/3EO1.01.01.5
SLS1.01.01.5
Sodium sarcosinate3.53.54.0
Glycerine0.90.90.9
Lactic acid8.08.07.0
Formic acid1.01.00.0
Ethanol00.50.5
WaterBal.Bal.Bal.
AppearanceCloudy solutionClear solutionClear solution
StabilityPhase separationStableStable

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Patent 2024
Acids Amino Acids Ethanol formic acid Formic Acids Glycerin Lactic Acid Lupus Erythematosus, Systemic Microbicides Sodium Sodium Sarcosinate Stabilizing Agents Surface-Active Agents

Example 2

Thuricide BT Caterpillar Control (Southern Ag) was used as the source of viable Bacillus thuringiensis spores (6 million spores/mg). A dilution series was produced from Thuricide BT to show that the material is viable and could be readily cultured on Petrifilm plates. Three DEE chemical compositions were evaluated: (1) about 0.06 M copper (II) chloride in water, (2) about 1 wt.-% surfactant and about 10 wt.-% PCSR in water, and (3) about 1 wt.-% surfactant and about 1 wt.-% PCSR in water. OxiClean was used as the PCSR and Tween 80 as the surfactant. During testing of each DEE composition, the DEE composition was added to the spores to yield a 1:100 dilution of spores and exposed to 2.45 GHz microwave radiation for about 10 s. After exposure, the cells were centrifuged and washed to remove the DEE composition and then plated on Petrifilm and cultured for 24 h at 30° C. When using each of the three DEE compositions shown above, the decontamination method destroyed BT spores at 6-7 log kill levels and demonstrated the efficacy of bleach-free treatments.

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Patent 2024
Bacillus thuringiensis Cells chemical composition Chlorides Copper Decontamination Microwaves Spores Surface-Active Agents Technique, Dilution Thuricide Tween 80

Example 6

Table 6 demonstrated a synergistic effect between C1-8 organic acids and amino acid based surfactant against Candida albicans under the standard test EN13624, wherein the organic acids were a mixture of lactic acid and formic acid, the amino acid based surfactant was sodium sarcosinate, and the stabilizing agent was ethanol.

TABLE 6
FormulationLMNOP
IngredientsOn 100%On 100%On 100%On 100%On 100%
Organic Acids5.100.55.48.1
on 100% active
Sodium sarcosinate,09999
30%
Ethanol, 95%5.25.25.25.25.2
Glycerine, 87%11111
SLES 2EO, 28%(1)99999
SLS, 30%99999
WaterBal.Bal.Bal.Bal.Bal.
Micro Efficiency<1<11.382.004.18
against
Candida Albicans
(Log reduction)
(1)SLES 2EO is Sodium lauryl ether sulfate, 2EO
(2)SLS is Sodium laureth sulfate

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Patent 2024
Acids Amino Acids Candida albicans Ethanol Ethers formic acid Glycerin Lactic Acid lauryl ether sulfate Lupus Erythematosus, Systemic Microbicides Sodium sodium laureth sulfate Sodium Sarcosinate Stabilizing Agents Sulfate, Sodium Dodecyl Surface-Active Agents

Top products related to «Surface-Active Agents»

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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.
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The Biacore 3000 is a label-free, real-time biosensor system designed for the analysis of biomolecular interactions. The system utilizes surface plasmon resonance (SPR) technology to monitor interactions between immobilized molecules and molecules in solution, providing quantitative kinetic and affinity data.
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Sodium dodecyl sulfate (SDS) is a commonly used anionic detergent for various laboratory applications. It is a white, crystalline powder that has the ability to denature proteins by disrupting non-covalent bonds. SDS is widely used in biochemical and molecular biology techniques, such as protein electrophoresis, Western blotting, and cell lysis.
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The CM5 sensor chip is a core component of the GE Healthcare's label-free detection platform. It is designed to measure biomolecular interactions in real-time without the need for labeling. The CM5 chip surface is made of a carboxymethylated dextran matrix that allows for the immobilization of a wide range of biomolecules, enabling the study of various types of interactions.
Sourced in United States, United Kingdom, Morocco, Germany
RapiGest SF surfactant is a water-soluble reagent used for the rapid and efficient extraction and solubilization of proteins from biological samples. It is designed to facilitate the preparation of samples for analysis, particularly in mass spectrometry applications.
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Surfactant P20 is a laboratory reagent used in various scientific applications. It is a non-ionic detergent that functions as a surfactant, reducing the surface tension of liquids. Surfactant P20 is commonly used in biochemical and cell biology experiments to solubilize and stabilize proteins and other biomolecules.
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The Biacore X100 is a label-free, real-time interaction analysis system used for studying molecular interactions. It measures the binding between molecules in a sample and a target molecule immobilized on a sensor surface. The instrument provides kinetic and affinity data to support various applications, including drug discovery, antibody characterization, and protein-protein interaction studies.
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
Sourced in Sweden, United States, United Kingdom, France
The Biacore T100 is a label-free interaction analysis system that measures real-time interactions between biomolecules. It provides quantitative data on affinity, kinetics, and specificity of molecular interactions.
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BIAevaluation software is a data analysis tool developed by GE Healthcare. It is designed to process and analyze data generated from Biacore biosensor systems, which are used for label-free interaction analysis. The software provides functionalities for data processing, evaluation, and presentation.

More about "Surface-Active Agents"

Surface-active agents, also known as surfactants, are a class of versatile compounds that play a crucial role in a wide range of industrial and consumer applications.
These compounds, derived from natural sources like plant oils or animal fats, or synthetically produced, have the ability to lower the surface tension of liquids, enabling easier spreading and penetration.
Surfactants find use in a variety of products, including detergents, emulsifiers, wetting agents, and dispersants.
Their unique properties make them invaluable in enhancing the effectiveness and efficiency of many processes and formulations.
Researchers can optimize their surface-active agent studies using cutting-edge tools like PubCompare.ai, a leading AI-driven platform that helps identify the best protocols and products from literature, preprints, and patents.
This innovative solution streamlines the research process and improves the reproducibility and accuracy of findings.
In the study of surface-active agents, researchers may leverage various analytical techniques and instruments, such as the Biacore T200, Biacore 3000, and Biacore X100 systems, which utilize surface plasmon resonance (SPR) technology to analyze biomolecular interactions.
Additionally, the use of sodium dodecyl sulfate (SDS) and Surfactant P20, as well as the RapiGest SF surfactant and Triton X-100, can provide valuable insights into the properties and behavior of these compounds.
By harnessing the power of AI-driven platforms like PubCompare.ai, along with a comprehensive understanding of surface-active agents and their applications, researchers can optimize their studies, streamline their workflows, and enhance the quality of their findings.
This knowledge can lead to advancements in a wide range of industries, from detergents and personal care products to pharmaceutical and biotechnology applications.