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Endocytosis

Endocytosis is a fundamental cellular process in which materials are brought into the cell through the invagination of the cell membrane.
This process is essential for a variety of biological functions, including nutrient uptake, signaling, and immune response.
Endocytosis involves the formation of vesicles that pinch off from the cell surface and transport their cargo into the cell's interior.
There are several different types of endocytosis, including clathrin-mediated, caveolae-mediated, and macropinocytosis, each with its own unique characteristics and mechanisms.
Understanding the complexities of endocytosis is crucial for advancing research in fields such as cell biology, physiology, and pharmacology.
Leveraging AI-driven comparisons of published literature, preprints, and patents can help optimize endocytosis research and enhance reproducibility and accuracy in your studies.

Most cited protocols related to «Endocytosis»

The number of organisms or latex beads that were endocytosed or cell-associated with the various host cells was determined using our standard differential fluorescence assay [5 (link),7 (link),9 (link),51 (link)]. The host cells were grown to 95% confluency onto 12-mm diameter coverslips coated with fibronectin in 24-well tissue-culture plates. They were incubated with 105C. albicans hyphae in RPMI 1640 medium. After 45 min, the cells were rinsed twice with Hank's balanced salt solution (HBSS; Irvine Scientific) in a standardized manner and then fixed with 3% paraformaldehyde. In experiments performed with C. albicans, the adherent but nonendocytosed organisms were labeled with rabbit polyclonal anti–C. albicans antibodies (Biodesign International, http://www.biodesign.com) that had been conjugated with Alexa 568 (Invitrogen), which fluoresces red. Next, the cells were permeablized with 0.5% Triton X-100 (Sigma-Aldrich) in PBS, and then the cell-associated organisms (the endocytosed plus nonendocytosed organisms) were labeled with the anti–C. albicans antibodies conjugated with Alexa 488 (Invitrogen), which fluoresces green. The coverslips were viewed using an epifluorescent microscope, and the number of endocytosed organisms was determined by subtracting the number of nonendocytosed organisms (which fluoresced red) from the number of cell-associated organisms (which fluoresced green). At least 100 organisms were examined on each coverslip, and the results were expressed as the number of endocytosed or cell-associated organisms per high-powered field.
Experiments investigating the endocytosis and adherence of the yellow-green fluorescing latex beads were performed similarly, except that 3 × 105 beads were added to each well. The adherent, nonendocytosed control beads coated with biotinylated BSA were labeled with strepavidin Alexa 568. The adherent beads coated with either rAls1-N or rAls3-N were detected by indirect immunofluorescence using rabbit polyclonal anti-Als1 antibodies followed by Alexa 568–conjugated goat anti-rabbit antibodies.
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Publication 2007
alexa 568 Amyotrophic lateral sclerosis 1 Anti-Antibodies anti-c antibody Biological Assay Cells Endocytosis Fibronectins Fluorescence Goat Hanks Balanced Salt Solution Hemoglobin, Sickle Hyphae Indirect Immunofluorescence Latex Microscopy paraform Rabbits Streptavidin Tissues Triton X-100
To measure macropinocytosis, serum-starved A431 cells grown on coverslips and placed in Chamlid chambers were incubated with 0.5 mg/ml TMR-dextran and, where noted, stimulated with 100–200 ng/ml EGF in the indicated buffer for 10 min at 37°C. Cells were washed and both DIC and red fluorescence images of live cells were acquired. Where indicated, the following inhibitors were used: 10 µM latrunculin B, 100 µM LY294002, 1 mM amiloride, or 10 µM HOE-694. In the case of latrunculin B and LY294002 the cells were preincubated with the inhibitors at 37°C for 30 min before EGF addition. Macropinocytosis was quantified as the number of cells containing macropinosomes in the cells outlining each island.
Endocytosis was assessed by incubating the cells with 50 µg/ml Alexa 546–conjugated transferrin in the indicated buffer for 15 min at 37°C, after which the cells were placed on ice and acid washed with 0.2 M acetic acid in 150 mM NaCl and PBS to remove exofacial fluorescence. The cells were then fixed and mounted on slides, and red fluorescence was imaged and quantified.
Publication 2010
Acetic Acid Acids Amiloride Buffers Cells Dextran Endocytosis Erythrocytes Fluorescence HOE 694 inhibitors latrunculin B LY 294002 Serum Sodium Chloride Transferrin
Excitation scans were generated using a Deltascan dual-wavelength fluorimeter from Photon Technology International (PTI; Birmingham, NJ) and the associated Felix software. Standard HEK293 cells were plated on 10 cm dishes and transiently transfected with 5 µg each of the soluble forms of GFP2, pHluorin and pHluorin2 using Fugene HD (Roche, Indianapolis, IN). Forty-eight hours post transfection, cells were washed with Hank’s Balanced Salt solution lacking calcium and magnesium ions and containing 2 mM EDTA. Cells were lifted from the plates using the same solution after a 10 minute incubation at 37°C and placed in a quartz cuvette with a stir bar. Excitation scans were performed between wavelengths 370 nm to 490 nm with the emission set at 510 nm. For the pH clamp experiments, cells were resuspended in a buffer containing 140 mM potassium chloride, 10 mM sodium phosphate with molar ratios of mono- and dibasic forms appropriate for the given pH and 30 mM nigericin (EMD Biosciences, Gibbstown, NJ). For the florescence plate reader studies, black, 96-well plates (Perkin-Elmer, Boston, MA) were loaded with 25,000 cells per well from the transfections described above and analyzed with dual excitation at 405 nm/8 nm and 485 nm/25 nm with a 535 nm/25 nm emission filter in an EnVision plate reader (Perkin-Elmer, Boston, MA). The narrow bandwidth of the 405 nm filter of 8 nm reduces the relative florescence compared to the larger bandwidth of the 485 nm filter. Despite this effect, the 405/485 nm ratios are still responsive to changes in intracellular pH.
For the hPTH1R endocytosis studies, HEK293 cells were sparsely plated into culture slides and transiently transfected with 100 ng of the hPTH1R-pHluorin2 construct using Fugene HD. Forty-eight hours post-transfection, cells were treated with either vehicle (acetic acid) or 100 nM parathyroid hormone containing amino acids 1 to 34 for 20 minutes. Cells were fixed with 3.7% paraformaldehyde and analyzed by confocal microscopy using a Radiance 2100 confocal microscope and the associated LaserSharp 2000 software (Bio-Rad Laboratories, Inc., Hercules, CA).
Publication 2011
Acetic Acid Amino Acids Buffers Calcium Cells Edetic Acid Endocytosis FuGene HEK293 Cells Hyperostosis, Diffuse Idiopathic Skeletal Ions Magnesium Microscopy, Confocal Molar Nigericin paraform Parathyroid Hormone PHluorin Potassium Chloride Protoplasm Quartz Radionuclide Imaging Sodium Chloride sodium phosphate Transfection
The study was designed to examine the contribution of SP-induced endocytosis of the NK1R to signal transduction in subcellular compartments, excitation of spinal neurons, and nociception. Endocytosis of the NK1R was examined in HEK293 cells by using BRET to assess the proximity between the NK1R and proteins resident in the plasma membrane and early endosomes and by localizing fluorescent SP by confocal microscopy. BRET was also used to examine the assembly of signaling complexes, which were localized in endosomes by immunofluorescence and super-resolution microscopy. Signaling in subcellular compartments of HEK293 cells was studied by expressing genetically encoded FRET biosensors, which allowed analysis of signaling with high spatial and temporal fidelity. NK1R endocytosis was studied in spinal neurons in slice preparations and in vivo by immunofluorescence and confocal microscopy. To examine the excitation of pain-transmitting neurons, cell-attached patch clamp recordings were made from second-order neurons in slices of rat spinal cord. Nociceptive behavior was evaluated in conscious mice after intraplantar administration of capsaicin, formalin, or CFA. To examine the contribution of NK1R endocytosis to signaling, neuronal excitation, and nociception, HEK293 cells, rat spinal cord slices, or mice were treated with pharmacological or genetic inhibitors of clathrin, dynamin, or βARRs, or with peptide inhibitors of NK1R/βARR interactions. Peptidic and small-molecule antagonists of the NK1R were conjugated to the lipid cholestanol, which facilitated endosomal targeting and retention of antagonists. Cholestanol-conjugated antagonists were used to directly evaluate the contribution of NK1R signaling in endosomes to SP-induced compartmentalized signaling in HEK293 cells, excitation of spinal neurons, and nociception. Institutional Animal Care and Use Committees approved all studies.
Publication 2017
Aftercare antagonists Biosensors Capsaicin Cell Membrane Proteins Cells Cholestanol Clathrin Consciousness Dynamins Endocytic Vesicles Endocytosis Endosomes Fluorescence Resonance Energy Transfer Formalin HEK293 Cells Immunofluorescence inhibitors Institutional Animal Care and Use Committees Lipids Microscopy Microscopy, Confocal Mus Neurons Nociception Pain Peptides Reproduction Retention (Psychology) Spinal Cord
We recently characterized a labeling process for plasma membrane-localized KCa3.1 using BLAP-tagged channels in combination with recombinant BirA [28 ]. Briefly, cells were washed in PBS, followed by incubation in recombinant BirA for 30 min at room temperature, three PBS washes, incubation in streptavidin (10 μg/ml in PBS with BSA 1% ) at 4°C for 10 min and three washes in PBS with BSA 1% to remove unbound streptavidin. While this provides excellent labeling of channels, it takes nearly 50 min to complete and therefore needed to be streamlined for adaptation to a 96-well plate application. In light of this, we subcloned both BLAP-tagged KCa3.1 as well as BirA, in which a KDEL endoplasmic reticulum-retention motif (BirA-KDEL) had been added at the C-terminus (kindly provided in pDISPLAY), into the bicistronic plasmid, pBudCE4.1 (Invitrogen) behind the EF-1α and CMV promoters, respectively. BirA-KDEL was directly subcloned from pDISPLAY using Sal I and Hind III restriction sites. We then introduced a silent mutation into the Kpn I site that was transferred from the pDISPLAY vector during this cloning step. Finally, BLAP-KCa3.1 was PCR amplified from pcDNA3.1 and Kpn I, and Xho I restriction sites added in a single step and subcloned into pBudCE4.1 containing BirA-KDEL. Stable HEK293 cell lines were then selected using zeocin. With this approach, each subunit of the channel was biotinylated in the endoplasmic reticulum as it was synthesized via a covalent modification, resulting in a greater biotinylation efficiency compared with the addition of recombinant BirA. Cells expressing BirA-KDEL and KCa3.1-BLAP were seeded at a density of approximately 50% confluence (16 h prior to the experiment) into Nunc 96-well optical bottom black plates (Nalge Nunc International, Rochester, NY), which have been previously poly L-lysine coated. To ensure the highest biotinylation efficiency possible, 10-μM biotin was added to the growth media when the cells were seeded to eliminate the possibility that biotin supply is rate limiting.
To label plasma membrane channels, the growth media was removed, the cells were washed once with PBS with BSA 1% and the channels were labeled in a single step with streptavidin–Alexa555 (10 μg/ml in PBS with BSA 1%) at 4°C for 10 min followed by three washes in PBS with BSA 1% to remove unbound streptavidin. In this way, the total labeling time was reduced to approximately 12–15 min compared with the 50 min previously required. Cells treated in this way serve as controls (time = 0 min) in which all the channel is localized to the plasma membrane. To assess endocytosis of the channel, a subset of plates is returned to 37°C for 90 min in the absence or presence of the compound in order to be tested for its ability to inhibit endocytosis. We previously demonstrated that 90 min is sufficient to endocytose most of the labeled KCa3.1 in both HEK293 and endothelial cells [28 , Balut CM, Gao Y, Thibodeau PH, Murray SA, Devor DC. ESCRT-dependent targeting of plasma membrane localized KCa3.1 to the lysosomes. Manuscript Submitted]. It is important to note that the binding of streptavidin to biotin is essentially irreversible, with a Ka of 1015 M−1, such that it will stay attached to the channel throughout its endocytosis and subsequent degradation. To adapt our endocytosis assay to an automated analysis system we labeled the plasma membrane with WGA–Alexa488 (wheat germ agglutinin, 5 μg/ml, Invitrogen) in PBS with BSA 1% at 4°C, either at time 0 or after 90 min. Importantly, this WGA-labeling step is carried out prior to the cells being fixed and permeabilized, such that only the plasma membrane was labeled. For this, the cells are either immediately incubated in WGA–Alexa488 (time 0) or the growth medium is first removed and the cells washed once in PBS with BSA 1% (time 90 min) prior to WGA–Alexa488 labeling. Subsequently, the cells are washed three times in PBS with BSA 1% and once in PBS at 4°C to remove unbound WGA. This protocol allowed us to unequivocally define the membrane fluorescently and thus colocalize the channel with the plasma membrane as a means of assessing endocytosis. Subsequent to WGA-Alexa488 labeling, the cells were fixed and permeabilized in paraformaldehyde 2% with Triton X-100 0.1% for 15 min and the nuclei labeled with DAPI for 30 s. A schematic depicting this protocol and the labeling of plasma membrane channels is shown in Figure 1. Also shown is a high-resolution image at both time 0 and 90 min to illustrate the labeling of both KCa3.1 with streptavidin–Alexa555 and the plasma membrane with WGA–Alexa488 (Figure 2). As is apparent, at time 0, all of the channel is resident in the plasma membrane and colocalizes with WGA (the plasma membrane marker). After 90 min at 37°C, the majority of KCa3.1 has been endocytosed resulting in less colocalization with WGA–Alexa488.
Following labeling, individual cells within each well of the 96-well plate were imaged using a Nikon TiE inverted, widefield epifluoresence microscope with Plan–Neofluor objectives, a motorized six-position fluorescent filter cube turret with zero-pixel shift filters and a registered motorized stage with plate insert. The 12-bit grayscale images were captured using a Retiga 2000 camera (QImaging) and Volocity Acquisition software (v5.3.1, Perkin Elmer) that autofocused on the plasma membrane using the WGA–Alexa488 fluorescence, automatically capturing four to ten images per well. For these studies we utilized a 20× air objective with an numerical aperature of 0.5. Under the experimental conditions, both cellular autofluorescence and the autofluorescence associated with UBEI-41 were negligible and eliminated by thresholding prior to image collection. Fields that failed to autofocus or which were devoid of cells were ignored. Images were analyzed using the Volocity Quantification module using the colocalization analysis feature. Under the imaging conditions employed, there are 0.738 μm per pixel in both the x and y planes. Colocalization between the red and green channels is expressed as a Pearson’s correlation where a value of 1 indicates complete colocalization and 0 indicates no colocalization. A Pearson’s correlation coefficient was calculated for each experimental condition by averaging the coefficients for individual imaged fields. Initially, at time 0, KCa3.1 was exclusively localized to the membrane such that the Pearson’s correlation was high. However, given that KCa3.1 did not occupy all membrane space, colocalization will be less than 100% and was determined by expression level. Clearly, a high level of expression is necessary to obtain a large signal-to-noise level for these experiments, such that endocytosis can be clearly defined relative to time 0. This was obtained by having a stable cell line that expresses KCa3.1 in all cells driven by the EF-1α promoter coupled with high-efficiency labeling of the channel with biotin by utilizing the BirA-KDEL driven off a CMV promoter. The minimal starting colocalization, which will allow us to clearly define small-molecule modulators of endocytosis, has not been defined. Following endocytosis, colocalization of KCa3.1 with membrane fluorescence will be reduced such that modulators of this event can be defined.
Publication 2010
Acclimatization Biological Assay Biotin Biotinylation Cardiac Arrest Cell Lines Cell Nucleus Cells Cloning Vectors Culture Media DAPI Endocytosis Endoplasmic Reticulum Endothelial Cells Fluorescence HEK293 Cells Ion Channel Lysine Lysosomes Microscopy Neofluor paraform Plasma Plasma Membrane Plasmids Poly A Protein Subunits Retention (Psychology) Silent Mutation Streptavidin Tissue, Membrane Training Programs Triton X-100 Wheat Germ Agglutinins Zeocin

Most recents protocols related to «Endocytosis»

A Tat-conjugated peptide, designed to block the binding of dynamin to amphiphysin and thus prevent endocytosis (Gout et al., 1993 (link); Lissin et al., 1998 (link); Kittler et al., 2000 (link); Lin et al., 2011 (link)), was infused in order to block endocytosis. Depending on the experiment, rats received bilateral infusions of Tat P4 peptide and Tat Scrambled control peptide (S) (60μg/μl/0.5 μl side; Cambridge, UK), human recombinant BDNF or saline (0.5 μg/μl/0.5 μl side), ANA-12 or saline at different times during the behavioral task. The injection volume was always 0.5 μl/side. Sequences are as follows: amino acid sequence for the dynamin inhibitory peptide (P4) is QVPSRPNRAP, and for the Scrambled control peptide (S) is QPPASNPRVR.
Bilateral infusions were conducted simultaneously using two 5-μl Hamilton syringes that were connected to the infusion cannulas by propylene tubing. Syringes were driven by a Harvard Apparatus precision syringe pump, which delivered 0.5 μl to each hemisphere over 1 min. The infusion cannulas were left in place for an additional minute to allow for diffusion. At least 3 days were allowed for washout between repeated infusions.
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Publication 2023
Amino Acid Sequence amphiphysin brain-derived neurotrophic factor, human Cannula Cardiac Arrest Diffusion Dynamins Endocytosis glutaminyl-valyl-prolyl-seryl-arginyl-prolyl-asparagyl-arginyl-alanyl-proline Gout peptide P4 Peptides propylene Rattus Saline Solution Syringes

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Publication 2023
ACE2 protein, human Antibodies, Neutralizing bafilomycin A Cardiac Arrest Cells Chloroquine Endocytosis HeLa Cells Hydroxychloroquine inhibitors Lens, Crystalline N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide
Chicken OVA labeled with Alexa Fluor 488 (AF488‐OVA) was used (Thermo Fisher) to detect the antigen uptake and endocytosis of bone marrow‐derived CD103+DCs of WT and IL‐37tg. Briefly, WT and IL‐37tg CD103+DCs were treated with poly(I:C) for 18 h. The control was not given any treatment. CD103+DCs were then incubated with AF488‐OVA (50ug/ml) at 37°C for 45 min, washed, and dead cells were labeled with 7‐AAD viability staining solution (BioLegend). The MFI of OVA‐AF488 in living cells was measured by flow cytometry. To measure the ability of OVA peptide presentation to MHC‐I, CD103+ DCs were treated with poly(I:C) for 18 h and incubated with OVA protein (50 ug/ml) at 37°C for 1 h. The cells were then washed with PBS, and stained with H2Kb‐APC (Biolegend) for about 15 min at room temperature. CD103+DCs without OVA treatment and isotype controls were used as negative control and staining controls separately. H2Kb levels were measured by flow cytometry.
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Publication 2023
alexa fluor 488 alpha HML-1 Antigens Bone Marrow Cells Chickens Egg Proteins Endocytosis Flow Cytometry Immunoglobulin Isotypes Peptides Poly I-C
The trajectories of sEVs were reconstructed from the original video stack with Imaging‐Pro‐Plus software (Media Cybernetics) by aligning the proximity and similarity in coordinate and intensity of each spots representing sEVs or corresponding structures in every frame. Only the trajectories within the focal plane were processed for quantitative analysis of single particle tracking. The MSD was calculated by the user‐written program with MATLAB software (MathWorks). The different motion modes were determined by fitting the dependence of MSD against time interval (Δt) with the formulas as below: MSD = 4DΔt + constant (free diffusion), MSD = 4DΔtα + constant (restricted diffusion) and MSD = 4DΔt + (VΔt)2 + constant (directed diffusion), where D and V represents the diffusion coefficient and the mean velocity respectively. The orthogonal slice view was obtained by UltraVIEW (PerkinElmer) to display the relative position of particles and cell in a 3D view. Kymograph analysis was performed with Image J. Line profile of colocalization or endocytosis were exhibited by using Imaging‐Pro Plus software.
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Publication 2023
Cells Diet, Formula Diffusion Endocytosis Exanthema Kymography Reading Frames
Murine brain endothelial (bEnd.3) cells were plated in a 12-well plate at a density of 150,000 per well in 1 ml of medium (DMEM, 10% fetal bovine serum (FBS), 1% penicillin/streptomycin). Once confluent, cells in treatment groups receiving ionizing radiation were exposed to 0.25 Gy XRT. After 1 h cells were collected, transferred to microcentrifuge tubes and fixed on ice using 2% paraformaldehyde. Fixed cells were washed twice with PBS and then resuspended in 100 μl of fluorescent activated cell sorter (FACS) buffer (PBS with 2% FBS). Cells were stained with 2 μl of anti-P-selectin antibody (Biolegend, no. 148310) and incubated at room temperature for 30 min. Cells were then washed twice with PBS, resuspended in 300 μl of FACS buffer and transferred to FACS tubes for analysis. Data were collected on a BD LSR II flow cytometer and analysed using either FCS Express Software (v.7.06) or FlowJo (v.10.6.1). To quantify the effects of endocytosis inhibitors on nanoparticle uptake, bEnd.3 cells were plated in a 12-well plate at a density of 150,000 per well in 1 ml of medium. On reaching confluency, cells were treated with medium containing chlorpromazine (5.00, 6.25, 7.50, 8.75 μg ml–1), methyl-β-cyclodextrin (5.00, 6.25, 7.50, 8.75 mM) or regular medium. After 8 h, cells were washed with PBS and treated with nanoparticles (1:100 dilution of FiVis in complete DMEM medium). Cells were incubated with nanoparticles for 30 min at 37 °C. Afterwards, cells were washed twice with PBS and resuspended in freshly prepared FACS buffer containing propidium iodide as a viability stain. Data were collected on a BD LSR II flow cytometer using the APC-Cy7 channel (excitation with a 633 nm red laser and detection with a 780/60 nm bandpass filter) to detect fluorescent signal from the infrared dyes within the nanoparticles. Data were analysed using FCS Express Software.
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Publication 2023
Antibodies, Anti-Idiotypic Brain Buffers Cells Cell Survival Chlorpromazine Cyclodextrins Decompression Sickness Endocytosis Endothelium Fluorescent Dyes inhibitors Mus P-Selectin paraform Penicillins Propidium Iodide Radiation, Ionizing Stains Streptomycin Technique, Dilution

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Dynasore is a small molecule compound used in laboratory research. It functions as a dynamin inhibitor, a protein involved in processes such as endocytosis. The core function of Dynasore is to inhibit the activity of dynamin, which is important for various cellular processes.
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Chlorpromazine is a pharmaceutical compound used as a laboratory reagent. It is a white crystalline solid that is soluble in water and organic solvents. Chlorpromazine is commonly used in research and laboratory settings as a reference standard or for various analytical purposes.
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The FACSCalibur is a flow cytometry system designed for multi-parameter analysis of cells and other particles. It features a blue (488 nm) and a red (635 nm) laser for excitation of fluorescent dyes. The instrument is capable of detecting forward scatter, side scatter, and up to four fluorescent parameters simultaneously.
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FM4-64 is a lipophilic styryl dye that is commonly used as a fluorescent membrane stain in biological research. It selectively labels the plasma membrane and can be used to visualize endocytic processes in live cells.
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Cytochalasin D is a laboratory reagent that inhibits actin polymerization. It is commonly used in cell biology research to disrupt the cytoskeleton and study its role in cellular processes.
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Nystatin is an antifungal medication used in the laboratory setting. It is a polyene macrolide antibiotic that functions by disrupting the cell membrane of fungal cells, leading to their death. Nystatin is commonly used for the treatment and prevention of fungal infections in in vitro experiments and laboratory procedures.
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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.
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More about "Endocytosis"

Endocytosis is a fundamental cellular process where materials are brought into the cell through the invagination of the cell membrane.
This essential process is involved in various biological functions, including nutrient uptake, signaling, and immune response.
Endocytosis involves the formation of vesicles that pinch off from the cell surface and transport their cargo into the cell's interior.
There are several types of endocytosis, such as clathrin-mediated, caveolae-mediated, and macropinocytosis, each with unique characteristics and mechanisms.
Understanding the complexities of this process is crucial for advancing research in fields like cell biology, physiology, and pharmacology.
Dynasore, a GTPase inhibitor, can be used to study clathrin-mediated endocytosis, while Chlorpromazine disrupts clathrin-coated pit formation.
The FACSCalibur flow cytometer can be utilized to analyze endocytic uptake, and the fluorescent dye FM4-64 can be employed to visualize endocytic vesicle formation.
Cytochalasin D, an actin polymerization inhibitor, can be used to investigate macropinocytosis, and Genistein, a tyrosine kinase inhibitor, can be applied to study caveolae-mediated endocytosis.
Additionally, Nystatin, a cholesterol-binding agent, can be used to disrupt caveolae-mediated endocytosis, and fetal bovine serum (FBS) can be a source of growth factors and other biomolecules that may influence endocytic processes.
The LSM 880 confocal microscope can provide high-resolution imaging of endocytic events, and Amiloride, a sodium-proton exchanger inhibitor, can be used to study macropinocytosis.
Leveraging AI-driven comparisons of published literature, preprints, and patents can help optimize endocytosis research and enhance reproducibility and accuracy in your studies.
Explore the latest advancements in the field and take your endocytosis research to new heights.