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Alginate

Alginates are natural polysaccharides derived from brown seaweeds.
They are composed of varying proportions of mannuronic and guluronic acid residues, which determine their physical and chemical properties.
Alginates have a wide range of applications in the biomedical, pharmaceutical, and food industries due to their biocompatibility, biodegradability, and ability to form hydrogels.
They are commonly used as thickening, stabilizing, and geling agents.
Alginates also have potential therapeutic uses, such as wound dressings, tissue engineering scaffolds, and drug delivery systems.
Reserach into the diverse applications of alginates is an active area of study.

Most cited protocols related to «Alginate»

1
Magnetic nanoparticle-based interstitial probes
Alginate probes were prepared using extrusion methods [18 (link)], [19 (link)]. Briefly, 1% sodium alginate in water functioned as the anionic solution and 2% calcium chloride containing 1% carboxymethylcellulose functioned as the cationic solution. Functionalized mNPs [12 ] (Micromod, 100 nm hydrodynamic diameter, iron oxide, dextran coated) were added to the cationic solution to achieve 1 mg/ml concentration. Droplets of the cationic solution were injected into 100 ml of anionic solution under constant stirring to generate hollow core beads. After alginate beads formed, they were rinsed with 2% calcium chloride three times, and incubated in 0.01% calcium solution at 4 °C. The resulting probes proved stable for two months. For spectroscopic measurements, calcium-alginated beads containing around 300 μg mNP were used.
We used blood as a surrogate for the interstitial in vivo environment. Blood contains most of the chemical complexities of the in vivo environment: the antibodies, enzymes, and a host of other proteins large and small present in vivo are all present in blood. Other biological samples are generally less problematic: urea, saliva, tissue, and so on. Blood is also the most commonly collected biological sample and has the most complicated composition. It has been shown that mNPs were readily taken in by cells resulting in a lower MSB signal [11 ]. Whole blood was harvested in an eppendorf tube containing heparin from the vena cava of euthanized C57BL/6 mice using a 3 mL syringe and a 25G needle. The whole blood was spun at 4500 r/min for 20 min at 4 °C, and the supernatant was used for experiments as plasma.
The spectroscopic measurements for the probe data were acquired at 1270 Hz on our original apparatus [9 ]–[12 ]. The ratio of the fifth over the third harmonics of the mNP magnetization was used as a concentration-independent metric [9 ], [10 (link)].
In the second arm of this paper, we tested the sensitivity of a recently introduced spectrometer that measures the magnetization perpendicular to the oscillating applied field. The perpendicular magnetization is induced by applying a small static field perpendicular to the oscillating applied field [20 (link)].
Zhang X., Reeves D., Shi Y., Gimi B., Nemani K.V., Perreard I.M., Toraya-Brown S., Fiering S, & Weaver J.B. (2015). Toward Localized In Vivo Biomarker Concentration Measurements. IEEE transactions on magnetics, 51(2), 1-4.
Publication 2015
Alginate Antibodies Biopharmaceuticals BLOOD Blood Substitutes Calcium, Dietary Calcium chloride Carboxymethylcellulose Cations Cells Dextran Enzymes ferric oxide Heparin Hydrodynamics Hypersensitivity Mice, Inbred C57BL Needles Plasma Saliva Sodium Alginate Spectrum Analysis Staphylococcal Protein A Syringes Tissues Urea Venae Cavae
2
Comprehensive Bacterial Genome Analysis for Biosynthetic Gene Clusters

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Publication 2014
Alginate Anabolism Gene Clusters Genes Genome Genome, Bacterial Lipopolysaccharides Pseudomonas fluorescens Salinispora tropica Streptomyces griseus
3
Rat Femoral Defect Model for Bone Regeneration

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Publication 2010
Alginate Animals Blood Vessel Bones Buprenorphine Cytoskeletal Filaments Diaphyses Femur Institutional Animal Care and Use Committees Needles Operative Surgical Procedures Pain PEGDMA Hydrogel polysulfone Rats, Sprague-Dawley Rattus norvegicus recombinant human bone morphogenetic protein-2 Seizures Stainless Steel Woman X-Ray Computed Tomography X-Rays, Diagnostic
4
Alginate-Encapsulated Colon Cancer Cell Culture
A detailed description of the cell cultivation in alginate is given by Shakibaei and de Souza [4 (link)]. Briefly, the pellet of HCT116 and HCT116R cells (1 × 106/ml) was resuspended in alginate (2% in 0.15 M NaCl, stirring for 1–2 h) and slowly added dropwise into a solution containing 100 mM CaCl2 at ambient temperature (AT). The alginate beads polymerized in the presence of CaCl2 after 10 min. Subsequently, the CaCl2 solution was removed and the alginate beads washed three times with 0.15 M NaCl solution and twice with serum-starved medium (3% FBS). Alginate beads were left untreated, treated with various concentrations of curcumin (0.1, 1, 5, 10, 20 μM), 5-FU (0.01, 0.1, 1, 10nM) or the combinational treatment of curcumin/5-FU (5 μM/0.01nM or 5 μM/0.1nM) in serum-starved medium, as previously described [26 (link)]. The medium was changed every 3 days. The cultures were grown in an incubator at 37°C with 5% CO2 in air.
Shakibaei M., Kraehe P., Popper B., Shayan P., Goel A, & Buhrmann C. (2015). Curcumin potentiates antitumor activity of 5-fluorouracil in a 3D alginate tumor microenvironment of colorectal cancer. BMC Cancer, 15, 250.
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Publication 2015
Alginate Cells Curcumin Serum Sodium Chloride
5
Kinetic Analysis of Alginate Lyase Activity
Reactions in 200 µl volumes were set up in triplicate in a 96 well quartz plate. Alginate, polyG, and polyM substrates were in 20 mM Tris, 200 mM NaCl, pH 8 buffer. Substrate concentrations ranging from 4 mg/ml to 0.0625 mg/ml using two-fold serial dilutions were assayed. The quartz plate and substrate were equilibrated to 50°C, followed by the addition of the enzyme to obtain a final protein concentration of 0.25 µg/ml. Initial velocities were determined from each reaction over a ten minute run. To determine enzyme kinetics, the averaged initial velocities in milli-absorbance units (mAU) at 235 nm per minute versus the substrate concentrations were determined. As alginate is a polymer of variable length consisting of random combinations of mannuronic acid and guluronic acid residues, and as both have the same molecular weight (MW), substrate molarity was calculated using the MW of 176 g/mol for each monomer of uronic acid in the polymer (i.e. 194 g/mol monomer MW – 18 g/mol for the loss of H2O during polymerization). Therefore, 4 mg/ml alginate is 22.7 mM monomer of uronic acid. Product concentrations were determined from the increase in absorbance at 235 nm using the extinction coefficient of 6150 M−1 cm−1[20] (link)–[22] (link). Velocity (V) at the tested substrate concentration was calculated as follows: V (mol/s)  =  (milliAU/min × min/60 sec × AU/1000milliAU × 1 cm)/(6150 M−1 cm−1) × (2 ×10−4 liters). Substrate molar concentrations and their associated velocity values were input in the Hyper32 program, http://homepage.ntlworld.com/john.easterby/hyper32.html[23] for calculating the maximal velocity, Vmax, and the Michaelis-Menten constant, Km, for each substrate using hyperbolic regression analysis. The turnover number, kcat, for AlgMsp was calculated as follows: kcat (s−1)  =  Vmax/E, where E is the mols of AlgMsp in the assay. Recombinant AlgMsp has a MW of 36,813 g/mol, therefore, at an enzyme concentration of 0.25 µg/ml, AlgMsp is equivalent to 6.79 nM, which is 1.36 pmol per 200 µl reaction.
Swift S.M., Hudgens J.W., Heselpoth R.D., Bales P.M, & Nelson D.C. (2014). Characterization of AlgMsp, an Alginate Lyase from Microbulbifer sp. 6532A. PLoS ONE, 9(11), e112939.
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Publication 2014
Alginate Biological Assay Buffers Enzymes Extinction, Psychological guluronic acid Kinetics mannuronic acid Molar Poly G Polymerization Polymers Quartz Sodium Chloride Staphylococcal Protein A Technique, Dilution Tromethamine Uronic Acids

Most recents protocols related to «Alginate»

1
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
2
Engineering Attenuated Pseudomonas Strain for Alginate
Not available on PMC !

Example 1

To generate an attenuated strain of P. aeruginosa for production of alginate, the following virulence factor genes were sequentially deleted from the chromosome of the wild-type strain PAO1: toxA, plcH, phzM, wapR, and aroA. toxA encodes the secreted toxin Exotoxin A, which inhibits protein synthesis in the host by deactivating elongation factor 2 (EF-2). plcH encodes the secreted toxin hemolytic phospholipase C, which acts as a surfactant and damages host cell membranes. phzM encodes phenazine-specific methyltransferase, an enzyme required for the production of the redox active, pro-inflammatory, blue-green secreted pigment, pyocyanin. wapR encodes a rhamnosyltransferase involved in synthesizing O-antigen, a component of lipopolysaccharide (LPS) of the outer membrane of the organism. aroA encodes 3-phosphoshikimate 1-carboxyvinyltransferase, which is required intracellularly for aromatic amino acid synthesis. Deletion of aroA from the P. aeruginosa genome has previously been shown to attenuate the pathogen. Each gene was successfully deleted using a homologous recombination strategy with the pEX100T-Not1 plasmid. The in-frame, marker-less deletion of these five gene sequences was verified by Sanger sequencing and by whole genome resequencing (FIG. 1 and FIG. 8). This engineered strain was designated as PGN5. The whole genome sequence of PGN5 has been deposited to NCBI Genbank with an accession number of CP032541. All five in-frame gene deletions were detected and validated to be the deletion as designed using PCR (FIG. 7).

To verify gene deletion and attenuation of the PGN5 strain, the presence of the products of the deleted genes was measured and was either undetectable, or significantly reduced in the PGN5 strain. To test for the toxA gene deletion in PGN5, a Western blot analysis was performed for the presence of Exotoxin A in the culture medium. Exotoxin A secretion was detected in wild-type PAO1 control, but not in the PGN5 strain (FIG. 2A). To confirm the loss of plcH, hemolysis was assessed on blood agar. The hemolytic assay was carried out by streaking PAO1, PGN5, P. aeruginosa mucoid strain VE2, and a negative control, Escherichia coli strain BL21 on blood agar plates. A clear zone was observed surrounding PAO1 and VE2 cell growth, indicating complete (β-) hemolysis (FIG. 2B). In contrast, the blood agar remained red and opaque surrounding PGN5 and BL21 growth, indicating negligible or no hemolytic activity in these strains (FIG. 2B). To assess for deletion of phzM, the amount of pyocyanin secreted by PAO1 and PGN5 was extracted and measured. The amount of pyocyanin detected was significantly reduced in PGN5 (FIG. 2C). In fact, the difference in pigment production between PAO1 and PGN5 was immediately apparent on agar plates (FIG. 3A-3B). To test for wapR gene deletion, an LPS extraction was performed, followed by silver-stained SDS-PAGE and Western blot on the following strains: PAO1, PGN4 (PGN5 without aroA deletion), VE2, and PAO1wbpL, which serves as a negative control due to a deletion in the O-antigen ligase gene, and thus produces no O-antigen. The presence of O-antigen was detected in PGN4, but the level of LPS banding was significantly reduced compared to the LPS banding profile observed in PAO1 and VE2 (FIG. 2D). Lastly, to test for aroA deletion, ELISA was performed to detect the presence of 3-phosphoshikimate 1-carboxyvinyltransferase in cell lysates prepared from PAO1 and PGN5. The ELISA results showed that the amount of 3-phosphoshikimate 1-carboxyvinyltransferase was significantly reduced in PGN5, compared to that in PAO1 (FIG. 2E). Additionally, the deletion of aroA resulted in slower growth in the PGN5 strain, a growth defect that was restored with the addition of 1 mg/mL of aromatic amino acids (W, Y, F) to the culture medium (data not shown).

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].
Full text: Click here
Patent 2024
1-Carboxyvinyltransferase, 3-Phosphoshikimate Agar Alginate Anabolism Aromatic Amino Acids Biological Assay BLOOD Cardiac Arrest Chromosomes Culture Media Deletion Mutation Enzyme-Linked Immunosorbent Assay Enzymes Escherichia coli Exotoxins Gene Deletion Genes Genetic Markers Genome Hemolysis Homologous Recombination Inflammation Ligase Lipopolysaccharides Methyltransferase O Antigens Oxidation-Reduction Pathogenicity Peptide Elongation Factor 2 Phenazines Phospholipase C Pigmentation Plasma Membrane Plasmids Protein Biosynthesis Pseudomonas aeruginosa Pyocyanine Reading Frames SDS-PAGE secretion SERPINA3 protein, human Silver Strains Surface-Active Agents Tissue, Membrane Toxins, Biological Virulence Factors Western Blot Western Blotting
3
Localization and Mortality in Mucoidal Strains
Not available on PMC !

Example 4

Since no mortality was observed in mice injected with PGN5+mucE, it was determined whether cells of this strain might localize differently than VE2 cells within the mice post-injection. To test this, the luxCDABEG operon was used to tag each strain with bioluminescence. VE2 and PGN5+mucE both carry gentamicin resistance genes, while the plasmids used for labeling with bioluminescence required gentamicin sensitivity. Thus, the luxCDABEG operon was incorporated into the chromosome of PAO1 and PGN5, and then the pUCP20-pGm-mucE plasmid was introduced into each strain to induce alginate production and mucoidy. Intraperitoneal injection of C57BL/6 mice with bioluminescent PAO1+mucE showed either localization at the injection site or dissemination through the body, and lethality resulted in all mice injected (FIGS. 5A-5B). Conversely, localization at the injection site but no dissemination was observed with bioluminescent PGN5+mucE, and no mortality was observed in injected mice (FIGS. 5C-5D).

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].
Full text: Click here
Patent 2024
Alginate Cells Chromosomes Cultured Cells Figs Genes Gentamicin Human Body Hypersensitivity Injections, Intraperitoneal Mice, Inbred C57BL Mus Operon Plasmids Strains
4
Calibrating Magnetic Stir Bar Agitation
One potentiometer coordinates an 8-bit PWM signal to the DC motor controller, with an effective maximum and minimum translational velocity of the lead screw assembly being 42.86 mm/s (255 PWM signal) and 14.77 mm/s (50 PWM signal—the minimum signal to power the DC motor). To ensure the velocity of the external magnets corresponds to the stir bar magnet velocity, an evaluation was performed. Stir bars were placed into separate syringes containing Hank’s Balanced Salt Solution (HBSS, Thermo Fisher Scientific) and alginate (LF200, FMC Polymer) media, representing different viscosities and resistances to translation of the stir bar magnet. Syringes were mounted to the Harvard Apparatus 33500TM syringe pump and the agitation system was activated at varying speeds. The stir bar motion within the syringe barrel was captured by video recording for each agitation condition. Captured videos were analyzed using a customized image analysis algorithm written in MATLAB (version 2015, MathWorks) for semi-automated measurement of kinetic linear velocity. The algorithm first auto-calibrates the spatial resolution of a video using the known stir bar principal dimension (5 mm) and then tracks user-inputted mouse clicks as frames are manually advanced. Each mouse click corresponds to an X-Y location in the frame of a defining feature for the stir bar (e.g., its lower-right corner) that remains consistent across frames and translation. Mouse clicks are tracked across frames to measure a linear distance and calculate a velocity. Six linear motions were tracked for each condition/video, with an average and standard deviation of velocities being calculated. The velocities correspond to kinetic motion of the stir bar after static friction was overcome.
Puttrich T., O’Donnell S., Wong S.W., Kotche M., Felder A.E, & Shin J.W. (2023). Development of a programmable magnetic agitation device to maintain colloidal suspension of cells during microfluidic syringe pump perfusion. PLOS ONE, 18(3), e0282563.
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Publication 2023
Alginate Friction Hemoglobin, Sickle Kinetics Mus Polymers Reading Frames Sodium Chloride Syringes Viscosity
5
Evaluating Cellular Suspension Maintenance
To test the ability of the agitation device to maintain cell suspension, detached cells were washed twice with HBSS and resuspended in either HBSS or 1% w/v high molecular weight (∼240 kDa) alginate (LF200; FMC Polymer) solution in complete DMEM at 5 million cells/mL. 500 μL of the cell suspension was loaded into a 1-mL syringe (4.78mm inner diameter; BD #309628). Syringes had a stir bar placed inside prior to loading of the cell suspension. The syringes were mounted to a Harvard Apparatus 33500TM syringe pump. The automated agitation device was assembled and mounted adjacent to the syringe pump. The syringe pump was set to perfuse 1 μL/min and the dispensed liquid was collected using Eppendorf tubes. Colloidal suspension concentrations were measured over two hours at the following time points: 0, 15, 30, 60, 90, and 120 min. Eppendorf tubes were replaced at every time point to preserve solution measurements. Four experimental agitation conditions were evaluated: no agitation, manual agitation, low-rate continuous agitation (velocity of ∼14 mm/s), and high-rate continuous agitation (∼42 mm/s). The manual agitation condition was applied by hand as previously described [6 (link)–9 (link)], and served as a positive control. Cell density of the dispensed solutions was determined via counting using a hemocytometer.
Puttrich T., O’Donnell S., Wong S.W., Kotche M., Felder A.E, & Shin J.W. (2023). Development of a programmable magnetic agitation device to maintain colloidal suspension of cells during microfluidic syringe pump perfusion. PLOS ONE, 18(3), e0282563.
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Publication 2023
Alginate Cells Hemoglobin, Sickle Medical Devices Polymers Syringes

Top products related to «Alginate»

1
Alginate by Merck Group
Sourced in United States, Germany, United Kingdom, Spain, France, Sweden, China, Italy
Alginate is a natural polymer derived from brown seaweed. It is a versatile material commonly used in various laboratory applications as a thickening, stabilizing, and gelling agent. Alginate provides structural support and can be used to create scaffolds for cell culture, tissue engineering, and drug delivery systems.
2
Sodium alginate by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, India, China, France, Spain, Poland, Canada, Israel, Saudi Arabia, Sao Tome and Principe, Czechia, Switzerland, Denmark, Macao, Taiwan, Province of China, Australia, Brazil, Singapore
Sodium alginate is a naturally-derived, water-soluble polysaccharide that is commonly used as a thickening, stabilizing, and gelling agent in various laboratory applications. It is extracted from brown seaweed and is known for its ability to form viscous solutions and gels when combined with water. Sodium alginate is a versatile material that can be utilized in a range of laboratory procedures and formulations.
3
Cacl2 by Merck Group
Sourced in United States, Germany, United Kingdom, Canada, France, Switzerland, Italy, China, Ireland, Israel, Spain, Sweden, India, Australia, Macao, Brazil, Poland, Sao Tome and Principe, Denmark, Belgium
CaCl2 is a chemical compound commonly known as calcium chloride. It is a white, crystalline solid that is highly soluble in water. CaCl2 is a versatile laboratory reagent used in various applications, such as precipitation reactions, desiccation, and control of ionic strength. Its core function is to provide a source of calcium ions (Ca2+) and chloride ions (Cl-) for experimental and analytical purposes.
4
Fetal bovine serum (fbs) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
5
Chitosan by Merck Group
Sourced in United States, Germany, United Kingdom, India, Italy, China, Poland, France, Spain, Sao Tome and Principe, Canada, Macao, Brazil, Singapore, Ireland, Iceland, Australia, Japan, Switzerland, Israel, Malaysia, Portugal, Mexico, Denmark, Egypt, Czechia, Belgium
Chitosan is a natural biopolymer derived from the exoskeletons of crustaceans, such as shrimp and crabs. It is a versatile material with various applications in the field of laboratory equipment. Chitosan exhibits unique properties, including biocompatibility, biodegradability, and antimicrobial activity. It can be utilized in the development of a wide range of lab equipment, such as filters, membranes, and sorbents, due to its ability to interact with various substances and its potential for customization.
6
Penicillin streptomycin by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, China, Canada, France, Japan, Australia, Switzerland, Israel, Italy, Belgium, Austria, Spain, Gabon, Ireland, New Zealand, Sweden, Netherlands, Denmark, Brazil, Macao, India, Singapore, Poland, Argentina, Cameroon, Uruguay, Morocco, Panama, Colombia, Holy See (Vatican City State), Hungary, Norway, Portugal, Mexico, Thailand, Palestine, State of, Finland, Moldova, Republic of, Jamaica, Czechia
Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
7
Gelatin by Merck Group
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Gelatin is a natural, water-soluble protein derived from the partial hydrolysis of collagen. It is commonly used as a gelling agent, thickener, and stabilizer in various food and pharmaceutical applications.
8
Calcium chloride by Merck Group
Sourced in United States, Germany, United Kingdom, India, Italy, Spain, China, France, Macao, Canada, Sao Tome and Principe, Switzerland, Belgium, Japan, Norway, Brazil, Singapore, Australia
Calcium chloride is a salt compound that is commonly used in various laboratory applications. It is a white, crystalline solid that is highly soluble in water. The core function of calcium chloride is to serve as a desiccant, absorbing moisture from the surrounding environment. It is also used as a source of calcium ions in chemical reactions and analyses.
9
Sodium chloride (nacl) by Merck Group
Sourced in United States, Germany, United Kingdom, India, Italy, France, Spain, China, Canada, Sao Tome and Principe, Poland, Belgium, Australia, Switzerland, Macao, Denmark, Ireland, Brazil, Japan, Hungary, Sweden, Netherlands, Czechia, Portugal, Israel, Singapore, Norway, Cameroon, Malaysia, Greece, Austria, Chile, Indonesia
NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.
10
Alginate lyase by Merck Group
Sourced in United States, Japan, United Kingdom
Alginate lyase is an enzyme that cleaves the glycosidic bonds in alginate, a polysaccharide found in the cell walls of brown algae. It catalyzes the depolymerization of alginate, breaking down the polymer into smaller units. The core function of alginate lyase is to facilitate the degradation and modification of alginate molecules.

More about "Alginate"

Alginates are naturally derived polysaccharides found in brown seaweeds.
They are composed of varying ratios of mannuronic and guluronic acid residues, which dictate their physical and chemical properties.
These versatile biopolymers have a wide range of applications in the biomedical, pharmaceutical, and food industries due to their biocompatibility, biodegradability, and ability to form hydrogels.
Alginates are commonly used as thickening, stabilizing, and gelling agents, and they also have potential therapeutic uses such as wound dressings, tissue engineering scaffolds, and drug delivery systems.
Sodium alginate is a common form of alginate that is widely used in these applications.
Calcium chloride (CaCl2) is often used in conjunction with alginates to form hydrogels, and fetal bovine serum (FBS) and chitosan are sometimes incorporated to further enhance the properties of alginate-based materials.
Alginate lyase is an enzyme that can be used to degrade alginates, which can be useful for certain applications.
Researchers are actively exploring the diverse applications of alginates, including the development of novel alginate-based products and the optimization of existing protocols.
By leveraging the power of AI-driven platforms like PubCompare.ai, researchers can easily locate and compare protocols from literature, pre-prints, and patents, ensuring reproducibility and accuracy in their alginate-related studies.