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Gels

Gels are semi-solid, gelatinous substances that can be used in a variety of applications, such as in cosmetics, pharmaceuticals, and biotechnology.
They are typically composed of cross-linked polymers that trap liquid within their three-dimensional network, resulting in a substance that is more viscous than a liquid but less rigid than a solid.
Gels can be classified based on their composition, such as hydorgels, organogels, and aerogels.
Researchers can use PubCompare.ai to locate the best gel protocols from literature, preprints, and patents, enhancing their research accuracy and reproducibility.
This AI-powered platform can help optimize experiments and unlock new insigths related to gels and their applications.

Most cited protocols related to «Gels»

Detailed eCLIP Experiment Protocol

(See Supplementary Protocol 1 for detailed Standard Operating Procedures for ENCODE-style eCLIP experiments, including oligonucleotide sequences, catalog numbers for all reagents, and specific details for eCLIP experiments). RNA binding protein (RBP)-RNA interactions were stabilized with UV crosslinking (254 nm, 400 mJ/cm²), followed by lysis in iCLIP lysis buffer, limited digestion with RNase I (Ambion), immunoprecipitation of RBP-RNA complexes with a specific primary antibody of interest using magnetic beads with pre-coupled secondary antibody (typically M-280 Sheep Anti-Rabbit IgG Dynabeads, ThermoFisher Scientific 11204D), and stringent washes. After dephosphorylation with FastAP (ThermoFisher) and T4 PNK (NEB), a barcoded RNA adapter was ligated to the 3′ end (T4 RNA Ligase, NEB) (at this step, multiple replicates of the same RBP, or potentially RBPs of similar size and bound RNA amount, can be uniquely barcoded and pooled after ligation to simplify downstream steps - see Supplementary Fig. 2a). Ligations were performed on-bead (to allow washing away unincorporated adapter) in high concentration of PEG8000, which improves ligation efficiency to > 90%. Samples were then run on standard protein gels and transferred to nitrocellulose membranes, and a region 75 kDa (~150 nt of RNA) above the protein size was isolated and proteinase K (NEB) treated to isolate RNA. RNA was reverse transcribed with AffinityScript (Agilent), and treated with ExoSAP-IT (Affymetrix) to remove excess oligonucleotides. A second DNA adapter (containing a random-mer of 5 (N₅) or 10 (N₁₀) random bases at the 5′ end) was then ligated to the cDNA fragment 3′ end (T4 RNA Ligase, NEB), performed with high concentration of PEG8000 (to improve ligation efficiency) and DMSO (to decrease inhibition of ligation due to secondary structure). After cleanup (Dynabeads MyOne Silane, ThermoFisher), an aliquot of each sample was first subjected to qPCR (to identify the proper number of PCR cycles), and then the remainder was PCR amplified (Q5, NEB) and size selected via agarose gel electrophoresis. Samples were sequenced on the Illumina HiSeq 2500 or 4000 platform as two Paired End 50bp (for N₅) or 55bp (for N₁₀) reads. All analyses were performed using identical antibody lots for RBFOX2 (A300-864A lot 002, Bethyl), SLBP (RN045P lot 001, MBL International), and IgG Isotype Control (02-6102 lot 32013, Thermo Fisher Scientific). SLBP experiments were performed with 20×10⁶ cells and 10 ug of primary antibody; RBFOX2 experiments were performed with 20×10⁶ cells and 10 ug (eCLIP Rep1 and Rep2) or 10×10⁶ cells and 5 ug (RNase I variation experiments). All experiments in K562 and HepG2 cells were performed with 20×10⁶ cells and 10 ug of indicated primary antibody (Supplementary Table 2). Antibody validation documentation (including Western images of immunoprecipitation and shRNA knockdown^{19 (link)}) are available at http://www.encodeproject.org/. Additional experiments performed in K562 and HepG2 cells in which the antibody failed to successfully immunoprecipitate the targeted RBP were excluded from analysis. 293T cells were obtained from Clontech (Lenti-X 293T cell line). K562 and HepG2 cells were purchased from ATCC, and were not independently verified. Cells were routinely tested for mycoplasma using MycoAlert PLUS (Lonza).

Van Nostrand E.L., Pratt G.A., Shishkin A.A., Gelboin-Burkhart C., Fang M.Y., Sundararaman B., Blue S.M., Nguyen T.B., Surka C., Elkins K., Stanton R., Rigo F., Guttman M, & Yeo G.W. (2016). Robust transcriptome-wide discovery of RNA binding protein binding sites with enhanced CLIP (eCLIP). Nature methods, 13(6), 508-514.

Publication 2016

anti-IgG Buffers Cell Lines Cells Digestion DNA, Complementary Domestic Sheep Electrophoresis, Agar Gel Endopeptidase K Gels HEK293 Cells Hep G2 Cells Immunoglobulin Isotypes Immunoglobulins Immunoprecipitation Ligation M 280 Mycoplasma Nitrocellulose Oligonucleotides polyethylene glycol 8000 Proteins Psychological Inhibition Rabbits Ribonuclease, Pancreatic RNA-Binding Proteins RNA Ligase (ATP) Short Hairpin RNA Silanes Sulfoxide, Dimethyl Tissue, Membrane

Detecting SINE200 Insertions Across Anopheles Genome

Genomic DNA was extracted with various standard procedures, and specimens were identified to species and molecular forms by PCR-RFLP [38 (link),39 (link)]. SINE200 elements were located in silico by BLASTN searches on the genome sequence of the A. gambiae PEST genome using the obtained SINE200 consensus sequence as a query. Thirteen SINE200 insertions lying within the A. gambiae molecular form speciation islands (sensu Turner [11 (link)]) on X, 2L and 2R chromosomes, and characterized by the presence of 500 bp flanking regions showing a single hit in the genome, were selected. Primers were designed to amplify across the element using Primer 3 software [40 (link)]. The selected loci were named 'S200' followed by the abbreviation of the chromosomal arm (2L, 2R, X), by a number/letter corresponding to the chromosomal location on the cytogenetic map [4 (link)] and by an additional number aimed to distinguish primer sets positioned on the same chromosome division. Genes annotated within a 20 Kb genome sequence including SINE200 insertions for each locus were retrieved from the PEST genome ver. Agam P3 Feb. 2006 (Table 2).
PCR reactions were carried out in a 25 μl reaction which contained 1 pmol of each primer, 0.2 mM of each dNTP, 1.5 mM MgCl2, 2.5 U Taq polymerase, and 0.5 μl of template DNA extracted from a single mosquito. Thermocycler conditions were 94°C for 10 min followed by thirty-five cycles of 94°C for 30 s, 54°C for 30 s and 72°C for 1 min., with a final elongation at 72°C for 10 min, and a 4°C hold. The resulting products were analysed on 1.5% agarose gels stained with ethidium bromide, with low and high molecular weight bands corresponding to fragments containing or lacking the targeted SINE200, respectively.
PCR products representing 'filled' and 'empty' sites of S200 X6.1 locus on X chromosome were sequenced on both strands using ABI Big Dye Terminator v.2 chemistry and an ABI Prism 3700 DNA Analyser. Multiple alignments were performed using ClustalX [37 (link)]. All sequences were deposited in GenBank under accession numbers EU881868–EU881887.
Indices of polymorphism (i.e. SINE200 insertion frequency and heterozygosity) and differentiation (Fst) at polymorphic loci were computed using Fstat 2.9.3.2 [41 ]. Significance was tested with Bonferroni-adjusted P-values, using the randomization approach implemented in Fstat.

Santolamazza F., Mancini E., Simard F., Qi Y., Tu Z, & della Torre A. (2008). Insertion polymorphisms of SINE200 retrotransposons within speciation islands of Anopheles gambiae molecular forms. Malaria Journal, 7, 163.

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Publication 2008

2-(2-(2-chloro-3-(2-(3,3-dimethyl-5-sulfo-1-(4-sulfo-butyl)-3H-indol-2-yl)-vinyl)-cyclohex-2-enylidene)-ethylidene)-3,3-dimethyl-1-(4-sulfo-butyl)-2,3-dihydro-1H-indole-5-carboxylic acid Chromosomes Chromosome Segregation Consensus Sequence Culicidae Ethidium Bromide Gels Genes Genetic Polymorphism Genome Heterozygote Magnesium Chloride Neutrophil Oligonucleotide Primers Plague prisma Restriction Fragment Length Polymorphism Sepharose Taq Polymerase X Chromosome

DNA Origami Scaffold Purification

Each sample was prepared by combining 20 nM scaffold (p7560 or p8064, derived from M13mp18), 100 nM of each staple oligonucleotide, buffer and salts including 5 mM Tris, 1 mM EDTA (pH 7.9 at 20°C), and 22 mM MgCl₂, except for the 30-helix-per-x-raster block, which was folded with 15 mM MgCl₂. Folding was carried out by rapid heat denaturation followed by slow cooling from 80 to 61°C over 80 min, then 60 to 24°C over 173 h. Samples were electrophoresed on 2% agarose gels (0.5× TBE, 11 mM MgCl₂, 0.5 μg/ml ethidium bromide) at 70 V for 4 h in an ice-water bath. Leading monomer bands were visualized with ultraviolet light, physically excised, crushed with a pestle (17 (link)) and filtered through a cellulose-acetate spin column for 3 min at 15 000 × g, 4°C.

Douglas S.M., Marblestone A.H., Teerapittayanon S., Vazquez A., Church G.M, & Shih W.M. (2009). Rapid prototyping of 3D DNA-origami shapes with caDNAno. Nucleic Acids Research, 37(15), 5001-5006.

Publication 2009

acetylcellulose Bath Buffers Edetic Acid Ethidium Bromide Gels Helix (Snails) Magnesium Chloride Oligonucleotides Salts Sepharose Staple, Surgical Strains Tromethamine Ultraviolet Rays

miRNA Sequencing and Expression Analysis

For miRNA sequencing, 5 µg of total RNA form each sample was ligated with both a 5′ adapter and 3′ adapter for reverse transcription using Superscript II at 42°C for 1 h and 70°C for 15 min. Subsequently, the reverse transcribed products were amplified using the following PCR program: a 15-cycle reaction at 98°C for 30 sec, followed by 15 cycles of 98°C for 10 sec, 72°C for 15 sec, and then 72°C for 10 min. After obtaining a ∼92-bp DNA band on 6% PAGE gels, the PCR products were ethanol precipitated and purified using Spin-X filter columns. Finally, miRNA libraries were sequenced on the Illumina Cluster Station and Genome Analyzer II following the manufacturer's protocol.
Low quality reads were trimmed and adapter sequences were accurately clipped with the aid of a dynamic programming algorithm before subsequent statistical analysis. After elimination of the duplicate reads, the remaining reads of at least 18 nt were mapped to a human reference genome (hg19) using SOAP V2.0. To remove tags originating from protein-coding genes, repeat sequences, rRNA, tRNA, snRNA, and snoRNA, we also mapped the short read tags to UCSC RefGene, RepeatMasker and NCBI Refseq, as well as our in-house ncRNA annotation datasets compiled from the NCBI GenBank database (http://www.ncbi.nih.gov). The same pipeline used for DGE mRNA differential expression analysis was also used for miRNA expression analysis.

Zhou L., Chen J., Li Z., Li X., Hu X., Huang Y., Zhao X., Liang C., Wang Y., Sun L., Shi M., Xu X., Shen F., Chen M., Han Z., Peng Z., Zhai Q., Chen J., Zhang Z., Yang R., Ye J., Guan Z., Yang H., Gui Y., Wang J., Cai Z, & Zhang X. (2010). Integrated Profiling of MicroRNAs and mRNAs: MicroRNAs Located on Xq27.3 Associate with Clear Cell Renal Cell Carcinoma. PLoS ONE, 5(12), e15224.

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Publication 2010

DNA, A-Form Ethanol Gels Gene Products, Protein Genome Genome, Human Homo sapiens MicroRNAs Repetitive Region Reverse Transcription Ribosomal RNA RNA, Messenger RNA, Untranslated Small Nuclear RNA Small Nucleolar RNA Transfer RNA

RNA Extraction and Transcriptional Analysis

Total RNAs were extracted using standard hot phenol RNA preparation method (51 (link)). For RT-PCR analysis, 1.5 µg of total RNAs were subjected to reverse transcription (RT) using gene-specific primers, and then the resulting cDNAs were analysed by standard PCR method or qPCR. Primers used are listed in Supplementary Table S3. The half-life of pre-mRNAs was determined as described previously (52 (link),53 (link)). For northern blotting, the procedures were as previously described (50 (link)) except that total RNAs (10 µg) were separated by 6% acrylamide gels. Sequences of oligonucleotide probes are listed in Supplementary Table S3. Band intensities were quantified using ImageJ densitometry software.

Kong K.Y., Tang H.M., Pan K., Huang Z., Lee T.H., Hinnebusch A.G., Jin D.Y, & Wong C.M. (2013). Cotranscriptional recruitment of yeast TRAMP complex to intronic sequences promotes optimal pre-mRNA splicing. Nucleic Acids Research, 42(1), 643-660.

Publication 2013

Acrylamide Densitometry DNA, Complementary Gels Genes mRNA Precursor Oligonucleotide Primers Oligonucleotide Probes Phenol Reverse Transcription RNA Standard Preparations

Most recents protocols related to «Gels»

Engineered Alginate Production in P. aeruginosa

Not available on PMC !

Example 2

PAO1, the parent strain of PGN5, is a wild-type P. aeruginosa strain that produces relatively small amounts of alginate and exhibits a non-mucoid phenotype; thus, PGN5 is also non-mucoid when cultured (FIG. 3A). In PAO1, the alginate biosynthetic operon, which contains genes required for alginate production, is negatively regulated. Activation of this operon leads to alginate production and a mucoid phenotype. For example, over-expression of mucE, an activator of the alginate biosynthetic pathway, induces a strong mucoid phenotype in the PAO1 strain (e.g., P. aeruginosa strain VE2; FIG. 3B). The plasmid pUCP20-pGm-mucE, which constitutively over-expresses MucE, was used to test whether the genetically-modified PGN5 strain could produce alginate. Indeed, the presence of this plasmid in PGN5 (PGN5+mucE) induced a mucoid phenotype (FIG. 3B). To measure the amount of alginate produced by PGN5+mucE on a cellular level, a standard carbazole assay was performed, which showed that the PGN5+mucE and VE2 (i.e., PAO1+mucE) strains produce comparable amounts of alginate (FIG. 3C; 80-120 g/L wet weight).

To examine whether the alginate produced by PGN5+mucE was similar in composition to alginate produced by VE2, HPLC was performed to compare the M and G content of alginate produced by each strain. The chromatograms obtained from alginate prepared from VE2 and PGN5+mucE were identical (FIG. 3D), and the M:G ratios were comparable to a commercial alginate control (data not shown). To confirm that the physical properties of VE2 and PGN5+mucE alginates were also similar, alginate gels were prepared from alginate produced by each strain and the viscosity and yield stress was measured. The viscosities of VE2 and PGN5+mucE alginate gels were comparable at 73.58 and 72.12 mPa, respectively (FIG. 3E). Similarly, the yield stress of VE2 and PGN5+mucE alginate gels were comparable at 47.34 and 47.16 Pa, respectively (FIG. 3G).

US11873477B2. Bacterial cultures and methods for production of alginate (2024-01-16). Marshall University Research Corporation [US]. Inventors: Hongwei D. Yu [US], Meagan E. Valentine [US], Richard M. Niles [US], Thomas Ryan Withers [US], Brandon D. Kirby [US].

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Patent 2024

Alginate Alginates Anabolism Biological Assay Biosynthetic Pathways carbazole Cells Gels Genes High-Performance Liquid Chromatographies Operon Parent Phenotype Physical Processes Plasmids Pseudomonas aeruginosa Strains Viscosity

Green Tea Infused Silk Gel

Not available on PMC !

Example 10

Steps:

Green Tea PrepHeat 250 mL water to boil

Steep tea bag 2-3 minutes

with occasional stir

remove tea bag and let cool

Gel SolutionUse TFF-10-0047 (3.71% silk)

Prepdilute to 3% silk with water

dilute to 2% with green tea

add L-ascorbic acid

GelGelation occurred like standard

gel at room temperature

Green/yellow color

Green Tea scent

Solution Spec:2% silk solution

65 mL (35 ml of 3.71% silk, 8.3

mL water, 21.66 mL green tea)

0.43 gL-ascorbic acid

FIG. 92 is a table summarizing an embodiment of a caffeine gel of the present disclosure. A silk gel with 2% silk and 100 mg L-ascorbic acid/15 mL solution was created with the addition of 50 mg caffeine/15 mL solution. The gel has the exact appearance of standard L-ascorbic acid gels.

US11857663B2. Stable silk protein fragment compositions (2024-01-02). Evolved By Nature, Inc. [US]. Inventors: Gregory H. Altman [US], Rebecca L. Lacouture [US], Rachel Lee Dow [US], Rachel M. Lind [US], Dylan S. Haas [US].

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Patent 2024

Ascorbic Acid Caffeine Fast Green FCF Furuncles Gels Green Tea Pheromone Silk STEEP1 protein, human Technique, Dilution

Synthesis and Characterization of Polymer 14

Not available on PMC !

Example 14

[Figure (not displayed)]

Polymer 13 (0.250 g, 1.396 mmol) was placed in a RB flask under a nitrogen atmosphere. Compound 14-a (90 mg, 0.679 mmol) was dissolved in dry DMF (5 mL) under nitrogen atmosphere and added to polymer 13 with stirring. The reaction mixture was stirred for 90 min at RT under a nitrogen atmosphere before being filtered and washed with DMF (5×5 mL) and methanol (5×5 mL). The product was concentrated in vacuo to yield polymer 14 as off-white powdery solid. Weight=0.1852 g (52% yield). A Kaiser test was used to confirm presence of terminal amines (a reading at 570 nm equating to 1.86 nmol amine). FTIR: 3251 (N—H/O—H), 2915/2874 (C—H), 1649 (C═O, amide of coupled product), 1583 (C═O of CMC), 1405/1316/1262/1020. Elemental analysis: Expected of product if DoS of raw material were 0.7: Mass 519 g mol⁻¹: C 48%, H 5.8%, N 5.6%. Actual: C 42.8%, H 6.95%, N 4.25%. Therefore of all monomers, approximately 53% contain the linker group.

Solubility of Polymer 14 was determined in a similar manner as for compound 1-c. Data is shown below: x indicates insoluble material.

AfterAfter

SolventInitialheatingsonicationOvernight

pH 9 bufferxNot testedNot testedSlight swelling/gelling

over time; particles

well dispersed

US11865192B2. Modified wound dressings (2024-01-09). CONVATEC TECHNOLOGIES INC. [US]. Inventors: Lucy Ballamy [GB].

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Patent 2024

Amides Amines Atmosphere Buffers Gels Methanol Nitrogen Polymers Powder Solvents Spectroscopy, Fourier Transform Infrared

Green Tea and Silk Nanocomposite Gel

Not available on PMC !

Example 10

Steps:

- Green Tea Prep Heat 250 mL water to boil
  - Steep tea bag 2-3 minutes with occasional
  - stir
  - remove tea bag and let cool
- Gel Solution
- Prep Use TFF-10-0047 (3.71% silk)
  - dilute to 3% silk with water
  - dilute to 2% with green tea
  - add L-ascorbic acid
  - Gelation occurred like standard gel at room
- Gel temperature
  - Green/yellow color
  - Green Tea scent
- Solution Spec: 2% silk solution
  - 65 mL (35 ml of 3.71% silk, 8.3 mL water,
  - 21.66 mL green tea)
  - 0.43 g L-ascorbic acid

US11857664B2. Stable silk protein fragment compositions (2024-01-02). Evolved By Nature, Inc. [US]. Inventors: Gregory H. Altman [US], Rebecca L. Lacouture [US], Rachel Lee Dow [US], Rachel M. Lind [US], Dylan S. Haas [US].

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Patent 2024

Ascorbic Acid Caffeine Fast Green FCF Furuncles Gels Green Tea Pheromone Silk STEEP1 protein, human Technique, Dilution

Preparation of Gel Capsule Formulations

Not available on PMC !

Example 6

A gel mass can be prepared in order to encapsulate the pharmaceutical compositions of the various Examples herein.

Gel mass compositions were formulated and produced according to the following steps. Purified water (22.2 kg) and glycerin (10.8 kg) were charged into a stainless steel tank with mixing and heated to a temperature of 80±5° C. Hydrolyzed gelatin (1.8 kg) and gelatin 200 bloom limed bone, NF (24.0 kg) were then added to the water/glycerin mixture and were mixed until all solids were completely dissolved. This resulted in the formation of a gel mass. The resulting gel mass was de-gassed under vacuum. Coloring agents OPATINT® white (0.6 kg) and OPATINT® red (0.6 kg) were then added to the gel mass and the resultant was mixed for about 5 minutes. The resultant was then de-gassed under vacuum for a sufficient period of time and ultimately passed to an encapsulation device for preparation of gel capsules of the types disclosed herein.

US11865179B2. Progesterone formulations having a desirable PK profile (2024-01-09). TherapeuticsMD, Inc. [US]. Inventors: Janice Cacace [US], Peter H. R. Persicaner [US], Thorsteinn Thorsteinsson [US], Frederick Sancilio [US], Julia Amadio [US], Brian Bernick [US], Neda Irani [US].

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Patent 2024

Bones Capsule Coloring Agents Gelatins Gels Glycerin Medical Devices Pharmaceutical Preparations Progesterone Stainless Steel Vacuum

Top products related to «Gels»

Pvdf membrane by Merck Group

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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.

Trizol reagent by Thermo Fisher Scientific

Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand

TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

Nitrocellulose membrane by Bio-Rad

Sourced in United States, Germany, Italy, United Kingdom, Canada, France, China, Switzerland, Japan, Spain, Australia, Sweden, Portugal, Israel, Netherlands, Belgium

Nitrocellulose membranes are a type of laboratory equipment designed for use in protein detection and analysis techniques. These membranes serve as a support matrix for the immobilization of proteins, enabling various downstream applications such as Western blotting, dot blotting, and immunodetection.

Protease inhibitor cocktail by Merck Group

Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore

The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.

Protease inhibitor cocktail by Roche

Sourced in United States, Switzerland, Germany, China, United Kingdom, France, Canada, Japan, Italy, Australia, Austria, Sweden, Spain, Cameroon, India, Macao, Belgium, Israel

Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.

Pvdf membrane by Bio-Rad

Sourced in United States, Germany, China, United Kingdom, Japan, France, Canada, Spain, Italy, Australia, Switzerland, Austria, Belgium

PVDF membranes are a type of laboratory equipment used for protein transfer and detection in Western blot analysis. They provide a stable and durable surface for the immobilization of proteins, enabling effective identification and quantification of target proteins in complex biological samples.

Image lab software by Bio-Rad

Sourced in United States, China, Germany, United Kingdom, Italy, France, Canada, Australia, Belgium, Japan, Portugal, Sweden, Czechia, Switzerland, Spain

Image Lab software is a data analysis tool designed for use with Bio-Rad's gel and blot imaging systems. The software provides a user-friendly interface for capturing, analyzing, and processing images of gels, blots, and other samples.

Odyssey infrared imaging system by LI COR

Sourced in United States, Germany, United Kingdom, China, Italy, Niger, France, Netherlands, Austria, Australia, Liechtenstein

The Odyssey Infrared Imaging System is a versatile laboratory equipment designed for high-sensitivity detection and quantification of fluorescent and luminescent signals. The system utilizes infrared technology to capture and analyze various molecular targets, such as proteins, nucleic acids, and small molecules, in a range of sample types.

Pierce bca protein assay kit by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, China, Australia, Switzerland, France, Italy, Canada, Spain, Japan, Belgium, Sweden, Lithuania, Austria, Denmark, Poland, Ireland, Portugal, Finland, Czechia, Norway, Macao, India, Singapore

The Pierce BCA Protein Assay Kit is a colorimetric-based method for the quantification of total protein in a sample. It utilizes the bicinchoninic acid (BCA) reaction, where proteins reduce Cu2+ to Cu+ in an alkaline environment, and the resulting purple-colored reaction is measured spectrophotometrically.

Bca protein assay kit by Thermo Fisher Scientific

Sourced in United States, China, Germany, United Kingdom, Japan, Belgium, France, Switzerland, Italy, Canada, Australia, Sweden, Spain, Israel, Lithuania, Netherlands, Denmark, Finland, India, Singapore

The BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.

What are the common types of gels?

Gels can be classified into several types based on their composition, including hydrogels (water-based), organogels (organic solvent-based), and aerogels (gas-based). Each type has unique properties and applications, such as hydrogels being commonly used in biomedical and cosmetic applications, organogels in personal care products, and aerogels in insulation and filtration systems.

What are some common applications of gels?

Gels have a wide range of applications across various industries, including cosmetics (e.g., face masks, hair gels), pharmaceuticals (e.g., drug delivery systems, topical treatments), biotechnology (e.g., tissue engineering, cell culture matrices), and even in food and beverages (e.g., jellies, thickeners). Their ability to hold and release liquids makes them versatile for delivering active ingredients or providing structure and texture.

How can researchers use PubCompare.ai to optimize their gel-related experiments?

PubCompare.ai allows researchers to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform's AI-driven analysis can help researchers identify the most effective protocols related to gels for their specific research goals, highlighting key differences in protocol effectiveness and enabling them to choose the best option for reproducibility and accuracy. This can save time and improve the success of gel-based experiments.

What are some common challenges in working with gels?

One of the key challenges in working with gels is ensuring consistent and reproducible results, as their properties can be sensitive to factors like temperature, pH, and the presence of other ingredients or impurties. Researchers may also face difficulties in scaling up gel-based processes or in achieving the desired rheological properties for a particular application. Utilizing tools like PubCompare.ai can help address these challenges by identifying the most robust and optimized gel protocols from the literature.

How can PubCompare.ai help researchers compare and select the best gel protocols?

PubCompare.ai's AI-powered platform can assist researchers in locating the most effective gel protocols from literature, preprints, and patents. By leveraging machine learning to analyze and compare a wide range of gel-related protocols, the platform can help researchers identify the critical differences that impact protocol effectiveness and reproducibility. This enables researchers to make more informed decisions when selecting the optimal gel protocol for their specific research goals, saving time and enhancing the accuracy of their experiments.

More about "Gels"

Gels are a versatile class of semi-solid, gelatinous substances used in a wide range of applications, from cosmetics and pharmaceuticals to biotechnology.
These materials are typically composed of cross-linked polymers that trap liquid within their three-dimensional network, resulting in a substance that is more viscous than a liquid but less rigid than a solid.
Gels can be classified based on their composition, such as hydrogels, organogels, and aerogels.
Researchers can utilize the power of AI-driven platforms like PubCompare.ai to locate the best gel protocols from the literature, preprints, and patents, enhancing their research accuracy and reproducibility.
This platform can help optimize experiments and unlock new insights related to gels and their applications.
In addition to gels, researchers may also encounter other important materials in their work, such as PVDF (polyvinylidene fluoride) membranes, which are commonly used for protein transfer and detection in Western blotting; TRIzol reagent, a popular solution for RNA extraction; nitrocellulose membranes, which are widely used for protein immobilization; and protease inhibitor cocktails, which help preserve protein integrity during sample preparation.
To analyze and visualize their experimental data, researchers may rely on software tools like Image Lab and the Odyssey Infrared Imaging System.
Additionally, the Pierce BCA Protein Assay Kit and the BCA protein assay kit are widely used for the quantification of protein concentrations.
By leveraging these resources and technologies, researchers can enhance their ability to work with gels and other important materials, ultimately driving advancements in their fields of study.