Log In Sign up
The largest database of trusted experimental protocols
> Phenomena > Natural Phenomenon or Process > Osmotic Shock

Osmotic Shock

Osmotic Shock: A biological response triggered by sudden changes in extracellular osmolarity, leading to rapid alterations in cellular volume and ion concentrations.
This process can impact various cellular functions and is of interest in fields like cell biology, physiology, and biotechnology.
PubCompare.ai's AI-driven comparisons can help locate the best protocols and products across literature, pre-prints, and patents to optimize your Osmotic Shock research and enhance the reproducibility of your experiments.

Most cited protocols related to «Osmotic Shock»

1
Regulation of Cellular Dynamics and Cholesterol Homeostasis

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2011
apotransferrin Bos taurus Buffers CAV1 protein, human Cells Cholesterol Collagen Type I Culture Media Cytochalasin D Dexamethasone FuGene Gentamicin Glucose Golgi Apparatus HeLa Cells Homo sapiens Insulin jasplakinolide latrunculin A lipofectamine 2000 Muscle Cells N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide Osmotic Shock oxytocin, 1-desamino-(O-Et-Tyr)(2)- Pharmaceutical Preparations Phosphates Saline Solution Sodium Azide Technique, Dilution
2
Trypsin-Mediated Hemagglutinin Fusion Assay
HAb2 cells were treated by 5 μg/ml trypsin (Fluka, Buchs, Switzerland) for 10 min at room temperature to cleave HA0 into its fusion-competent HA1-S-S-HA2 form. For HA300a and BHA-PI cells, trypsin (5 μg/ml) was supplemented with neuraminidase (0.2 mg/ml; Sigma Chemical Co.) to improve binding of RBC. The enzymes were applied together for 10 min at room temperature. To terminate the reaction, HA-expressing cells were washed twice with complete medium containing 10% fetal serum. After two washings with PBS, cells were incubated for 10 min with a 1 ml suspension of RBC (0.05% hematocrit). HA-expressing cells with zero to two bound RBC per cell were washed three times with PBS to remove unbound RBC and then used. When measuring RBC binding to cells, several areas of the dish were selected. We screened at least 200 cells to find the average number of RBC bound to each HA-expressing cell.
Fusion was triggered by incubation of cells with PBS titrated by citrate to acidic pH. After low-pH treatment, acidic solution was replaced by PBS. Fusion extent was assayed by fluorescence microscopy more than 20 min after low-pH application as the ratio of dye-redistributed bound RBC to the total number of the bound RBC. Longer incubations (up to 2 h) did not increase the extent of fusion. We performed the fluorescence microscopy for lipid and content mixing either in a cold room at 4°C or at room temperature, as required.
For spectrofluorometric measurements (SLM-Aminco, Urbana, IL), excitation and emission wavelengths were 550 and 590 nm for R18, and 473 and 515 nm for NBD-taurine. The standard fusion assay was performed as in Chernomordik et al. (1997) (link). Suspensions of HA-expressing cells with bound RBC in PBS were placed into a thermostated fluorescence cuvette and stirred with a Teflon-coated flea. Citric acid was injected into the cuvette to lower pH to 4.9. The increase in fluorescence was normalized to that at infinite dilution of the probe by lysing cells with 0.06% SDS. Spectrofluorometry was also used to evaluate LPC incorporation into RBC membranes at different temperature from the decrease in R18 quenching caused by adding exogenous lipid to HAb2 cells with bound R18-labeled RBC (Chernomordik et al., 1997 (link)). To induce swelling of cells by applying hypotonic medium (osmotic shock), HA-expressing cells with bound RBC were placed into PBS diluted by H2O (1:3) as in Melikyan et al. (1995b) (link).
Each set of experiments for each graph presented here was repeated on at least three occasions with similar results. Presented data were averaged from the same set of experiments.
Chernomordik L.V., Frolov V.A., Leikina E., Bronk P, & Zimmerberg J. (1998). The Pathway of Membrane Fusion Catalyzed by Influenza Hemagglutinin: Restriction of Lipids, Hemifusion, and Lipidic Fusion Pore Formation. The Journal of Cell Biology, 140(6), 1369-1382.
Publication 1998
Acids Biological Assay Cells Citrates Citric Acid Cold Temperature Enzymes Fetus Fleas Fluorescence Fusions, Cell Hyperostosis, Diffuse Idiopathic Skeletal Lipids Microscopy, Fluorescence NBD-taurine Neuraminidase Osmotic Shock Serum Spectrometry, Fluorescence Technique, Dilution Teflon Tissue, Membrane Trypsin Volumes, Packed Erythrocyte
3
Steady-State Growth and Fixation of E. coli
Escherichia coli K12 cells were grown to steady state in glucose minimal medium (Gb1) containing 6.33 g of K2HPO4.3H2O, 2.95 g of KH2PO4, 1.05 g of (NH4)2SO4, 0.10 g of MgSO4.7H2O, 0.28 mg of FeSO4.7H2O, 7.1 mg of Ca(NO3)2.4H2O, 4 mg of thiamine, 4 g of glucose and 50 μg of required amino acids per liter pH 7.0 at 28°C. MC4100 (LMC500) requires Lys for growth in minimal medium. Absorbance was measured at 450 nm with a 300-T-1 spectrophotometer (Gilford Instrument Laboratories Inc.). Steady state growth was achieved by dilution of an over night culture 1:1000 in fresh prewarmed medium of 28°C. The cells were allowed to grow up to a density of 0.2 and then diluted again in prewarmed medium. This procedure was repeated during 40 generations of exponential growth. The mass doubling time of MC4100 is 80 min under these conditions. The overnight dilution was calculated using the equation: D=2t/Td(ODnowODdes) , where D is the required dilution of the culture to obtain the desired optical density (ODdes) after t minutes, and Td is the mass doubling time in min. ODnow is the optical density of the culture to be diluted. The steady state cultures were fixed by addition of a mixture of formaldehyde (f.c. 2.8%) and glutaraldehyde (f.c. 0.04%) to the shaking water bath. This gives an osmotic shock that does not affect the localization of membrane or cytosolic proteins (Hocking et al., 2012 (link); van der Ploeg et al., 2013 (link)). Unfortunately, periplasmic proteins that are freely diffusing are shocked toward the poles. Therefore, the procedure is not suitable for immunolabeling of periplasmic proteins and if used, their localization pattern should be verified using fluorescent protein (FP) fusions and live imaging.
Vischer N.O., Verheul J., Postma M., van den Berg van Saparoea B., Galli E., Natale P., Gerdes K., Luirink J., Vollmer W., Vicente M, & den Blaauwen T. (2015). Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJ. Frontiers in Microbiology, 6, 586.
Full text: Click here
Publication 2015
Amino Acids Bath Cells Cytosol Escherichia coli K12 Formaldehyde Glucose Glutaral Osmotic Shock Periplasmic Proteins potassium phosphate, dibasic Proteins Sulfate, Magnesium Technique, Dilution Thiamine Tissue, Membrane Vision
4
Purification and Characterization of Nanobodies
Nanobodies were cloned into the periplasmic expression vector pET26b, containing an amino terminal signal sequence and a carboxy-terminal 8×histidine tag and transformed into BL21(DE3) Rosetta2 E. coli (Novagen). Cells were induced in Terrific Broth at an OD600 of 0.8 with 1 mM IPTG and incubated with shaking at 22 °C for 24 hours. Periplasmic protein was obtained by osmotic shock and the nanobodies were purified using nickel–nitrilotriacetic acid (Ni-NTA) chromatography9 (link). For crystallography, Nb6B9 was digested overnight with 1:50 (w/w) carboxypeptidase A (Sigma) to remove the His tag, then purified by size exclusion chromatography over a Sephadex S200 size exclusion column.
Surface plasmon resonance experiments were conducted with a Biacore T100 at 25 °C. Protein concentrations were determined by 280 nm absorbance with a Nanodrop2000 spectrometer (Thermo Scientific). Biotinylated BI167107-bound β2AR was immobilized on an SA sensorchip (GE) at an Rmax of approximately 40 response units (RU). Biotinylated tiotropium-bound M2 muscarinic receptor was immobilized with an RU value matching that of the reference surface to control for nonspecific binding. Measurements were made using serial dilutions of Nb80 or Nb6B9 in HBSM (10 mM HEPES pH 7.4, 150 mM NaCl, 0.01% MNG) using single-cycle kinetics. All data were analyzed with the Biacore T100 evaluation software version 2.0 with a 1:1 Langmuir binding model.
Radioligand binding assays were performed using purified β2AR reconstituted into HDL particles comprised of apolipoprotein A1 and a 3:2 (mol:mol) mixture of POPC:POPG lipid22 (link). Binding experiments with G-protein were performed as previously described8 (link). Binding reactions were 500 μL in volume, and contained 50 fmol functional receptor, 0.5 nM 3H dihydroalprenolol (3H-DHA), 100 mM NaCl, 20 mM HEPES pH 7.5, 0.1% bovine serum albumin, and ligands and nanobodies as indicated. Reactions were mixed, then incubated for four hours at room temperature prior to filtration with a Brandel 48-well harvester onto a filter pre-treated with 0.1% polyethylenimine. Radioactivity was measured by liquid scintillation counting. All measurements were performed in triplicate, and are presented as means ± SEM.
Ring A.M., Manglik A., Kruse A.C., Enos M.D., Weis W.I., Garcia K.C, & Kobilka B.K. (2013). Adrenaline-activated structure of the β2-adrenoceptor stabilized by an engineered nanobody. Nature, 502(7472), 575-579.
Publication 2013
Apolipoprotein A-I BI167107 Carboxypeptidase A Cells Cloning Vectors Crystallography Dihydroalprenolol Escherichia coli Filtration GTP-Binding Proteins HEPES Histidine Isopropyl Thiogalactoside Kinetics Ligands Molecular Sieve Chromatography Muscarinic Acetylcholine Receptor nickel nitrilotriacetic acid Osmotic Shock Periplasm Polyethyleneimine Proteins Radioactivity Radioligand Assay sephadex Serum Albumin, Bovine Signal Peptides Sodium Chloride Surface Plasmon Resonance Technique, Dilution Tiotropium VHH Immunoglobulin Fragments
5
Recombinant Human Growth Hormone Expression

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2012
Amino Acid Sequence Ampicillin Buffers Cells Centrifugation Chromatography, Affinity Cloning Vectors Codon Escherichia coli Extinction, Psychological Hypertonic Solutions Hypotonic Solutions imidazole Isopropyl Thiogalactoside Osmotic Shock Periplasm polyhistidine Proteins SDS-PAGE Sodium Chloride Sucrose Sulfate, Magnesium Tromethamine

Most recents protocols related to «Osmotic Shock»

1
Expression and Purification of Recombinant Human RBP4
Human RBP4 expression and purification from Escherichia coli was accomplished essentially as described previously (Shi et al., 2017 (link)). Briefly, human RBP4 (hRBP4) cDNA was cloned into a pET3a expression vector and expressed in BL-21 DE3 cells according to a standard protocol. Bacterial cells were harvested and lysed by osmotic shock. Insoluble material was pelleted by centrifugation, washed, and solubilized in 7M guanidine hydrochloride and 10 mM dithiothreitol. After overnight incubation, insoluble material was removed by ultracentrifugation, and the supernatant was used for the hRBP4 refolding procedure. hRBP4 was refolded by the dropwise addition of solubilized material into a mixture containing 150 μCi of [11,12-3H]ROL ([3H]ROL) (PerkinElmer Life Sciences) and non-radiolabeled ROL (Sigma) at a final concentration of 1 mm. Refolded holo-hRBP4 was dialyzed against 10 mM Tris/HCl buffer, pH 8.0, and loaded onto a DE53 anion exchange chromatography column (Whatman, Piscataway, NJ). Holo-hRBP4 was eluted with linear gradient of NaCl (0–1M) in 10 mM Tris/HCl buffer, pH 8.0. Collected fractions were examined by SDS-PAGE and UV-visible spectroscopy to ensure a proper protein/retinoid ratio. Fractions containing at least 90% holo-hRBP4 were pooled together and concentrated in a Centricon centrifugal filter device (cut-off 10,000 Da) (Millipore, Billerica, MA) to 5 mg/mL. [3H]ROL was quantified in a scintillation counter (Beckman Coulter, Indianapolis, IN). Holo-hRBP4 aliquots were stored at −80°C until used.
Radhakrishnan R., Leung M., Solanki A.K, & Lobo G.P. (2023). Mapping of the extracellular RBP4 ligand binding domain on the RBPR2 receptor for Vitamin A transport. Frontiers in Cell and Developmental Biology, 11, 1105657.
Full text: Click here
Publication 2023
Anions Bacteria Cells Centrifugation Chromatography Cloning Vectors Dithiothreitol DNA, Complementary Escherichia coli Homo sapiens Hydrochloride, Guanidine Medical Devices Osmotic Shock Proteins RBP4 protein, human Retinoids Scintillation Counters SDS-PAGE Sodium Chloride Spectrum Analysis Tromethamine Ultracentrifugation
2
Chloroplast Isolation and Fractionation
Three weeks old Arabidopsis thaliana wild‐type (Col‐0 ecotype) or cmt1 (SALK_129037c, grown for 6 weeks) plants were grown onto soil under 12 h light and 12 h dark periods (120 μmol photons s−1·m−2 light intensity).
When isolating intact chloroplasts, the foliar tissue was ground in a kitchen blender with Isolation buffer (330 mm sorbitol, 50 mm HEPES pH 7.5, 2 mm EDTA, 1 mm MgCl2, 5 mm ascorbic acid) and filtered through one layer of gauze. This solution was centrifuged for 5 min at 1500 g and 4 °C to rescue the pellet and resuspend it in Washing buffer (330 mm sorbitol, 50 mm HEPES pH 7.5), which was loaded on percoll gradients of 40% percoll solution (330 mm sorbitol, 50 mm HEPES pH 7.6, 40% percoll) and 80% percoll solution (330 mm sorbitol, 50 mm HEPES pH 7.6, 80% percoll) and centrifuged for 5 min at 8000 g and 4 °C and the intact chloroplasts rescued to be washed with washing buffer.
For the separation of chloroplast into stroma and membrane fractions, the procedure skipped the percoll gradient and continued with resuspension of crude chloroplasts in osmotic shock buffer (0.6 m sucrose, 1 mm EDTA, 10 mm Tricine pH 7.9). The sample was then incubated on ice for 30 min under darkness and centrifuged for 1 h at 100 000 g and 4 °C to separate the soluble fraction (stroma) from the pellet (membranes).
Espinoza‐Corral R., Schwenkert S, & Schneider A. (2023). Characterization of the preferred cation cofactors of chloroplast protein kinases in Arabidopsis thaliana. FEBS Open Bio, 13(3), 511-518.
Full text: Click here
Publication 2023
Arabidopsis thalianas Ascorbic Acid Buffers Chloroplasts Darkness Ecotype Edetic Acid HEPES isolation Light Magnesium Chloride Osmotic Shock Percoll Plants Sorbitol Sucrose Tissue, Membrane Tissues tricine
3
Recombinant vNAR Protein Production
The positive pCOMB3X plasmid containing the His-tagged vNAR sequence was transformed into E. coli BL21 (DE3) cells. An isolated colony was grown in 3 mL of LB medium supplemented with 100 μg/mL ampicillin and incubated for 12 h at 37 °C and 250 rpm. The overnight culture was added to 250 mL of fresh medium with the same antibiotic concentration and further cultured under the same culture conditions. Once the culture reached an OD600nm = 0.7, expression was induced by adding 0.5 mL of IPTG 0.5 M (Sigma, I5502), followed by an incubation of 5 h at 37 °C at 250 rpm. The vNAR was isolated from periplasmic space by osmotic shock and used to make the first screening for expression and recognition ELISA assays. The periplasmic extract of the clone that met both requirements was filtered through a 0.2 μm and purified by IMAC (Thermo Fisher Scientific, 88221). The NiNTA column was equilibrated with wash buffer (20 mM imidazole, 50 mM NaPO4, 300 mM NaCl, pH 8.0), the periplasmic extract was loaded using a syringe at 1 mL/min constant flux and then washed with 10 mL of wash buffer. Bound His-tagged vNAR was eluted with 5 mL of elution buffer (250 mM imidazole, 50 mM NaPO4, 300 mM NaCl, pH 8.0) and collected in 1 mL fractions. Before proceeding with the ELISA assay, the fractions containing the vNAR were dialyzed extensively against 0.5X PBS. Fractions were quantified using the Micro BCA kit (Thermo Scientific, 23235) and analyzed by SDS-PAGE and western blotting. An SDS-TRICINE-PAGE was run at 120 V for 45 min and stained with Coomassie brilliant blue with the Precision plus protein™ Dual-color standards (BioRad, 1610394) as a molecular protein marker. For the western blot analysis, proteins were transferred from the gel to a nitrocellulose membrane for 1 h at 200 mA using a Trans-blot semi-dry electrophoretic transfer cell (BioRad, 1703940). The membrane was blocked with 3% BSA-PBS for 1 h at room temperature with constant agitation. After discarding the blocking solution, anti-His-HRP (Roche, 11965085001) diluted 1:1,000 in 1% BSA-PBS was added, followed by incubation for 1 h at 37 °C. The membrane was then washed thrice with PBST for 2 min, and proteins were made visible using an HRP color development reagent (BioRad, 1706534).
Burciaga-Flores M., Márquez-Aguirre A.L., Dueñas S., Gasperin-Bulbarela J., Licea-Navarro A.F, & Camacho-Villegas T.A. (2023). First pan-specific vNAR against human TGF-β as a potential therapeutic application: in silico modeling assessment. Scientific Reports, 13, 3596.
Full text: Click here
Publication 2023
Ampicillin Antibiotics Biological Assay Biological Markers brilliant blue G Buffers Cells Clone Cells Electrophoresis Enzyme-Linked Immunosorbent Assay Escherichia coli imidazole imidazole-4-acetic acid Isopropyl Thiogalactoside Nitrocellulose Osmotic Shock Periplasm Plasmids Proteins SDS-PAGE Sodium Chloride Syringes Tissue, Membrane tricine Western Blot
4
Salt Stress Response of Lemongrass
Lemongrass plants were maintained under two NaCl concentrations (160 and 240 mM). These concentrations were selected as per our earlier finding on the salt sensitivity of lemongrass plants (Mukarram et al., 2022c (link)). Salt treatments began 21 days after transplantation. NaCl concentrations were supplied as 300 mL of 40 mM NaCl solutions every alternate day to attain the final concentration and to avoid osmotic shock. The control group was supplied only with 300 mL of double distilled water.
Mukarram M., Khan M.M., Kurjak D., Lux A, & Corpas F.J. (2023). Silicon nanoparticles (SiNPs) restore photosynthesis and essential oil content by upgrading enzymatic antioxidant metabolism in lemongrass (Cymbopogon flexuosus) under salt stress. Frontiers in Plant Science, 14, 1116769.
Full text: Click here
Publication 2023
Cymbopogon nardus Hypersensitivity Osmotic Shock Plants Sodium Chloride Transplantation
5
Quantifying Bacterial Membrane Mechanics
ONIX B04A plates were loaded with medium and pre-warmed to 37 °C. Exponentially growing cells were incubated at 37 °C in fresh LB without shaking for 60 min before transitioning into experimental conditions and imaging. For spent medium assays, cells were perfused with spent LB subsequent to fresh LB. For oscillatory osmotic shock assays, cells were subjected to alternating hyperosmotic shocks of 400 mM sorbitol (Sigma-Aldrich, Cat. #S1876, dissolved in LB) and recovery without sorbitol, with a period of 2 min (1 min shock and 1 min recovery). For plasmolysis/lysis assays to measure OM stiffness, cells were subjected first to hyperosmotic shock with 1 M sorbitol in LB and then treated with 5% N-lauroylsarcosine sodium salt (MP biomedicals, Cat. #190289) to remove the OM. Cells were stained with 300 μM 3-[[(7-Hydroxy-2-oxo-2H-1-benzopyran-3-yl)carbonyl]amino]-D-alanine hydrocholoride (HADA, MedChemExpress, Cat. #HY-131045/CS-0124027) and perfused with 0.85X PBS prior to the osmotic shock.
Mikheyeva I.V., Sun J., Huang K.C, & Silhavy T.J. (2023). Mechanism of outer membrane destabilization by global reduction of protein content. bioRxiv.
Publication Preprint 2023
Alanine Benzopyrans Biological Assay Cells N-lauroylsarcosine Osmotic Shock Shock Sodium Sodium Chloride Sorbitol

Top products related to «Osmotic Shock»

1
Dc protein assay by Bio-Rad
Sourced in United States, Germany, United Kingdom, Canada, France, Australia, Sweden, Switzerland, Italy, Spain, Belgium, Netherlands, Finland
The DC Protein Assay is a colorimetric assay for the determination of protein concentration. It is based on the reaction of protein with an alkaline copper tartrate solution and Folin reagent, resulting in the reduction of the Folin reagent by the copper-treated proteins. The color change is measured spectrophotometrically, and the protein concentration is determined by comparison to a standard curve.
2
Ni nta agarose by Qiagen
Sourced in Germany, United States, United Kingdom, Netherlands, China, Switzerland, Italy, Canada, Spain, India
Ni-NTA agarose is a solid-phase affinity chromatography resin designed for the purification of recombinant proteins containing a histidine-tag. It consists of nickel-nitrilotriacetic acid (Ni-NTA) coupled to agarose beads, which selectively bind to the histidine-tagged proteins.
3
Calcein am by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Canada, Australia, Japan, China, France, Italy, Belgium, Austria, Portugal, Switzerland, Czechia, Spain
Calcein AM is a fluorescent dye used for cell viability and cytotoxicity assays. It is a cell-permeant dye that is non-fluorescent until it is hydrolyzed by intracellular esterases, at which point it becomes fluorescent and is retained within live cells.
4
Peroxidase conjugated anti flag antibody by Merck Group
The Peroxidase-conjugated anti-FLAG antibody is a laboratory reagent used for the detection and identification of proteins tagged with the FLAG peptide epitope. The antibody is conjugated to the enzyme horseradish peroxidase, which allows for colorimetric or chemiluminescent detection of the target protein in various applications, such as Western blotting, immunoprecipitation, and enzyme-linked immunosorbent assays (ELISA).
5
Dc protein assay kit by Bio-Rad
Sourced in United States, United Kingdom, Germany, Italy, Australia, Spain, China, Japan, France, Canada, Belgium, Czechia, Sweden
The DC protein assay kit is a colorimetric-based protein quantification method developed by Bio-Rad. It allows for the determination of protein concentration in aqueous solutions.
6
Sorbitol by Merck Group
Sourced in United States, Germany, United Kingdom, China, Denmark, France, Italy, New Zealand
Sorbitol is a sugar alcohol that is commonly used in various laboratory applications. It serves as a humectant, sweetener, and cryoprotectant in various formulations and processes. Sorbitol is a crystalline powder with a mild, sweet taste.
7
Dnase by Merck Group
Sourced in United States, Germany, United Kingdom, Switzerland, France, Italy, Canada, Spain, China, Sao Tome and Principe, Jersey, Australia, Macao
DNase is a type of enzyme that catalyzes the degradation of DNA. It functions by cleaving the phosphodiester bonds in the DNA backbone, effectively breaking down DNA molecules into smaller fragments.
8
Liberase tm by Roche
Sourced in Switzerland, Germany, United States, United Kingdom, France
Liberase TM is a blend of collagenase and neutral proteases, designed for effective and gentle tissue dissociation. It is a reliable solution for the isolation of primary cells from various tissues.
9
Pet24 vector by Thermo Fisher Scientific
The PET24 vector is a plasmid-based expression system designed for the production of recombinant proteins in Escherichia coli. It features a T7 promoter for high-level protein expression, and a polyhistidine tag sequence for protein purification. The vector is suitable for standard molecular biology techniques such as cloning, transformation, and protein expression.
10
Envision multiwell reader by PerkinElmer
The Envision multiwell reader is a high-performance microplate reader designed for a wide range of applications in life science research and drug discovery. It offers sensitive detection across multiple detection modes, including absorbance, fluorescence, and luminescence. The Envision provides reliable and reproducible results, enabling researchers to conduct a variety of assays with confidence.

More about "Osmotic Shock"

Osmotic shock, also known as hyperosmotic or hypo-osmotic stress, is a critical biological process that occurs when cells are suddenly exposed to changes in extracellular osmolarity.
This rapid alteration in the cell's surrounding environment can lead to dramatic shifts in cellular volume and ion concentrations, which in turn can impact a wide range of cellular functions and processes.
Osmotic stress is a key area of interest in fields like cell biology, physiology, and biotechnology.
Researchers studying osmotic shock may utilize techniques like the DC Protein Assay, Ni-NTA agarose, Calcein AM, and Peroxidase-conjugated anti-FLAG antibody to measure and analyze cellular responses.
The DC protein assay kit can be used to quantify protein concentrations, while Ni-NTA agarose and PET24 vector can be employed for protein purification and expression, respectively.
Compounds like Sorbitol, DNase, and Liberase TM can also play important roles in osmotic shock experiments, helping to manipulate the cellular environment and facilitate the extraction or lysis of cells.
The Envision multiwell reader, meanwhile, can be a valuable tool for high-throughput analysis of cellular responses to osmotic stress.
By understanding the key aspects of osmotic shock, researchers can optimize their experimental protocols, enhance the reproducibility of their findings, and ultimately advance our knowledge of this critical biological process and its implications across various fields of study.