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Tight Junction Proteins

Tight Junction Proteins are a critical component of the cellular junctions that regulate the permeability and transport of molecules across epithelial and endothelial cell layers.
These proteins play a key role in maintaining tissue integrity, barrier function, and cell-cell communication.
Researchers can leverage PubCompare.ai's AI-powered platform to easily locate, compare, and optimize research protocols for studying Tight Junction Proteins, accelerating their work and improving reproducibility.
This ultimate tool allows users to unlock the best approaches by analyzing protocols from literature, pre-prints, and patents, empowering researchers to advance their understanding of this important class of proteins.

Most cited protocols related to «Tight Junction Proteins»

1
Quantifying Brain Capillary Protein Levels
Cited 11 times

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Publication 2010
Actins Antibodies Blood Vessel Brain Capillaries Claudin-5 Collagen Type IV Densitometry Laminin Membrane, Basement Microvessels Occludin Plasma Proteins Plasmin Proteins Thrombin Tight Junction Proteins
2
FRAP and FLIP Analysis of Tight Junctions
Cited 8 times
MDCK cells were transfected and maintained as described previously (Shen and Turner, 2005 (link)) and were studied 3 d after confluence, except where otherwise indicated. Monolayers were transferred to bicarbonate-free HBSS supplemented with 15 mM Hepes, pH 7.4, at 37°C and mounted on a custom-designed temperature-controlled stage (Brook Industries) at 37°C for 30 min to allow equilibration. Confocal scanning light microscopy was performed by using a microscope system (TCS SP2 AOBS; Leica) with a 63× NA 1.40 oil immersion objective and a pinhole between 1 and 2 AU. EGFP fusion proteins were excited using the argon 488-nm laser line and emission gated between 490 and 530 nm. FRAP experiments were performed using the FRAP module of confocal software (Leica). A region of interest to be bleached was defined, and maximum laser power at the appropriate wavelength for an empirically determined number of iterations was used to bleach signals. Bleaching time was usually <10 s, resulting in bleaching throughout the full thickness of the tight junction. After bleaching, images were taken within the same focal plane at regular intervals (between 2 and 30 s) to monitor fluorescence recovery.
To test the continuity of different cellular pools of tight junction proteins, FLIP experiments were performed using the FLIP module of the confocal software. Observation and photobleaching were performed in the same scan for different regions of the scanning field. Continuous scanning was performed with no delay between scans for 5–15 min. For tight junction bleaching, a small area at the tight junction was continuously bleached at full laser power. For intracellular bleaching, a large area that encompasses ∼80% of the intracellular area at the tight junction level was continuously bleached at full laser power. In either case, the remainder of the field was observed using the laser at ∼10% power.
For inhibitor experiments, monolayers were treated with appropriate drugs in HBSS for 1 h before use. ATP depletion experiments were performed using glucose-free HBSS containing 2 mM 2-d-deoxy-glucose, 1 mM 2,4-dinitrophenol, and 10 mM NaN3 to inhibit ATP generation. MBCD was used at 5 mM.
Shen L., Weber C.R, & Turner J.R. (2008). The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. The Journal of Cell Biology, 181(4), 683-695.
Publication 2008
2-Deoxyglucose Argon Ion Lasers Bicarbonates Cardiac Arrest Cells Dinitrophenols enhanced green fluorescent protein Fluorescence Glucose Hemoglobin, Sickle HEPES Light Madin Darby Canine Kidney Cells Microscopy Microscopy, Confocal, Laser Scanning Pharmaceutical Preparations Protoplasm Radionuclide Imaging Sodium Azide Submersion Tight Junction Proteins Tight Junctions
3
Broiler Chicken Coccidiosis Challenge Study
Cited 6 times
The three treatments were allocated to cages in a completely randomized block (row of cages) design to give 12 replicates per treatment. Birds had free access to treatments and drinking water for 14 d; feed was replenished throughout the day and feed refusals were weighed daily, for determining cage feed intake. On d 5, birds (6 replicates per treatment on the left row of cages) were challenged with 1 mL of Eimeria culture (25,000 oocysts of E. acervulina and 5,000 oocysts of E. maxima) in distilled water suspension via oral gavage and the other 6 replicates (non-challenged control, on the right row of cages) were given equal volume of distilled water. The separation of right and left cages was an effort to minimize cross-contamination of non-challenge cages. Moreover, daily checks and servicing of the birds started with non-challenged birds followed by challenge birds. The Eimeria culture and challenge protocols were provided by Dr. John Barta of Department of Pathobiology, University of Guelph. Body weight and feed intake was monitored during pre- (d 0 to 5) and post- (d 6 to 14) challenge periods for calculation of BWG and FCR. Two birds per cage were Necropsied on d 10 for intestinal tissue samples. Jejunum was immediately located and excised at duodenal loop and 2 cm anterior to Markel diverticulum. Segments (∼3 cm) of mid-jejunum were excised and placed in buffered formalin for histomorphology analysis (Kiarie et al., 2007 (link)). Additional segments of mid-jejunum (∼1 cm) were placed in a 2 mL tube filled with 1.2 mL Ambion RNAlater (Life Technologies Inc., Burlington, ON, Canada). These samples were placed on ice and immediately transported to the lab and stored at −20°C until required for mRNA analysis of digestive enzymes, nutrients transporters, tight junction proteins, and cytokines. Lesion scores in intestinal regions (duodenum, jejunum, ileum, and ceca) were assessed blindly as described by Price et al. (2014 ) using a scale of 0 (none) to 4 (high) (Johnson and Reid, 1970 (link)). Excreta samples for apparent retention (AR) of components and oocyst shedding were collected from d 10 to 13. The excreta samples for oocyst counts were collected, stored at 4°C, and processed in accord with Price et al. (2014 ). The excreta samples for AR of components were frozen at −20°C until required for analyses. All birds were Necropsied by cervical dislocation on d 14 for gastrointestinal weight measurements
Kim E., Leung H., Akhtar N., Li J., Barta J.R., Wang Y., Yang C, & Kiarie E. (2017). Growth performance and gastrointestinal responses of broiler chickens fed corn-soybean meal diet without or with exogenous epidermal growth factor upon challenge with Eimeria. Poultry Science, 96(10), 3676-3686.
Publication 2017
Aves Body Weight Cecum Cytokine Digestion Diverticulum Duodenum Eimeria Enzymes Feed Intake Formalin Freezing Ileum Intestines Jejunum Joint Dislocations Membrane Transport Proteins Neck Nutrients Oocysts Retention (Psychology) RNA, Messenger Tight Junction Proteins Tissues Tube Feeding
4
Retinal Histology and Microscopy Techniques
Cited 6 times
Eyes were briefly fixed in 4% paraformaldehyde for 5 minutes and then anterior segments were removed. After post-fixation in 4% paraformaldehyde for 1 hour, eye cups were either transferred to PBS containing 30% sucrose and then embedded in optimal cutting temperature (OCT) compound for cryosection IHC, or placed in PBS for retinal flatmount IHC. For cryosection IHC, frozen sections were blocked with 5% normal goat serum and incubated with an antibody to GS (1:100; Chemicon International), cleaved-caspase 3 (1:100, Cell Signaling), SOX9 (1:200; Chemicon International), glial fibrillary acidic protein (GFAP, 1:250; Dako), collagen IV (1:250; ABD serotec), smooth muscle actin (SMA, 1:20; Dako), CD31 (1:50, BD) or VEGF-A (1:50, Santa Cruz). Bound antibodies were detected with Alexa Fluor 488 or 594-conjugated goat or donkey secondary antibodies (1:1000; Invitrogen).
For flatmount staining, dissected eye cups were fixed in 4% paraformaldehyde for 1 hour and then placed in PBS at +4°C overnight. On the next day, retinas were isolated, rinsed in PBS and permeabilized with 1% Triton-X-100 containing 5% normal goat serum blocking solution for at least 2 hours. Retinas were incubated in 100μl of solution containing fluorescence-conjugated- peanut-agglutinin (PNA, 10μg/ml; Invitrogen) to label cone photoreceptor outer segments (POS) or Griffonia simplicifolia isolectin B4 (IB4, 10μg/ml; Sigma) for retinal vessels in 0.1 M PBS with 1% BSA and 0.5% Triton X-100 overnight at +4°C. PNA labeled images were processed and quantitatively analyzed using computer-based image analysis software with customized macroroutines as described previously (Guidolin et al., 2004 (link); Shen et al., 2006 (link)).
To directly correlate retinal vascular abnormalities with photoreceptor injury, retinas were incubated with a cocktail consisting of Alexa Fluor 594-conjugated IB4 (10μg/ml; Invitrogen) and fluorescence-conjugated PNA (10μg/ml; Invitrogen). To correlate retinal vascular changes with alterations of tight junction protein claudin-5 expression, retinas were incubated with a cocktail consisting of Alexa Fluor 488-conjugated IB4 (10μg/ml; Invitrogen) and a rabbit polyclonal antibody to claudin-5 (1:100; Zymed). The bound antibody was detected with Alexa Fluor 594-conjugated secondary antibody (1:1000; Invitrogen). Retinas were flattened onto Superfrost-plus microscope slides and mounted for confocal laser scanning microscopy.
Shen W., Fruttiger M., Zhu L., Chung S.H., Barnett N.L., Kirk J.K., Lee S., Coorey N.J., Killingsworth M., Sherman L.S, & Gillies M.C. (2012). Conditional Müller Cell Ablation Causes Independent Neuronal and Vascular Pathologies in a Novel Transgenic Model. The Journal of Neuroscience, 32(45), 15715-15727.
Publication 2012
Actins Alexa594 alexa fluor 488 Antibodies Blood Vessel Caspase 3 Claudin-5 Collagen Type IV Congenital Abnormality Cryoultramicrotomy Equus asinus Fluorescence Frozen Sections Glial Fibrillary Acidic Protein Goat Griffonia simplicifolia isolectin B4 Immunoglobulins Injuries Microscopy Microscopy, Confocal paraform Peanut Agglutinin Photoreceptor Cells Rabbits Retina Retinal Cone Retinal Photoreceptor Cells Retinal Vessels Serum Smooth Muscles SOX9 protein, human Sucrose Tight Junction Proteins Triton X-100 Vascular Endothelial Growth Factors Vascular System Injuries
5
Impedance Spectroscopy for Accurate TEER Measurement
Cited 4 times
Impedance spectroscopy when combined with a fitting algorithm provides a more accurate representation of TEER values than traditional DC/single frequency AC measurement systems.34 (link) Impedance spectroscopy is performed by applying a small amplitude AC excitation signal with a frequency sweep and measuring the amplitude and phase response of the resulting current. Figure 2 (a) indicates a schematic which illustrates the concept of impedance measurement.
Electrical impedance (Z) is the ratio of the voltage-time function V (t) and the resulting current-time function I (t):
where Vo and Io are the peak voltage and current, f is the frequency, t is the time, Φ is the phase shift between the voltage-time and current-time functions, and Y is the complex conductance or admittance. Z is a complex function and can be described by the modulus |Z| and the phase shift Φ or by the real part ZR and the imaginary part ZI, as illustrated in the Figure 2(b). An in depth analysis of impedance spectroscopy has been published.35 Impedance measurement across a wide spectrum of frequencies instead of a DC/single frequency AC TEER measurement can provide additional information about the capacitance of the cell layer. An automated measurement system (cellZscope®, nanoAnalytics GmbH, Germany) has been developed for measuring the transendothelial/epithelial impedance of various barrier-forming cells cultured on permeable membranes of standard cell culture inserts. An equivalent circuit analysis of the measured impedance spectrum is performed to obtain the electrical parameters that can be applied to characterize the cellular barrier properties. Figure 3 (a) (adapted from Benson et al.26 (link)) shows a typical equivalent circuit diagram that can be applied to analyze the impedance spectrum of cellular systems.26 (link) In this circuit, the current can flow through the junctions between cells (paracellular route) or through the cell membrane of the cells (transcellular route). The tight junction proteins in the paracellular route contribute to an ohmic resistance (RTEER) in the equivalent circuit. Each lipid bilayer in the transcellular route contributes to a parallel circuit26 (link) consisting of ohmic resistance (Rmembrane) and an electrical capacitance (CC). In addition to these elements, the resistance of the cell culture medium (Rmedium) and the capacitance of the measurement electrodes (CE) also have to be considered. The high values of Rmembrane causes the current to mostly flow across the capacitor and allows an approximation where Rmembrane can be ignored26 (link) and the lipid bilayers can be represented with just CC. Based on this approximation, the equivalent circuit diagram can be further simplified as shown in Figure 3 (b) (adapted from Benson et al.26 (link)) and the impedance spectrum observed will have a non-linear frequency dependency as shown in Figure 3 (c) (adapted from Benson et al.26 (link)). Typically, there are three distinct frequency regions in the impedance spectrum where the impedance is dominated by certain equivalent circuit elements. In the low frequency range, the impedance signal is dominated by CE. In the mid frequency range, the impedance signal is dominated by circuit elements related to the cells, namely RTEER and CC. In the high frequency range, CC and CE provide a more conductive path and the impedance signal is dominated by Rmedium. These equivalent circuit parameters can be estimated by fitting the experimental impedance spectrum data to the equivalent circuit model using non-linear least squares fitting techniques to obtain the best fit parameters.
The following sections describe the advantages of organs-on-chips for TEER measurement, in vitro models of some widely studied cellular barriers, TEER measurements with in vitro models and some microfluidic implementations, and the various factors affecting TEER values.
Srinivasan B., Kolli A.R., Esch M.B., Abaci H.E., Shuler M.L, & Hickman J.J. (2015). TEER measurement techniques for in vitro barrier model systems. Journal of laboratory automation, 20(2), 107-126.
Publication 2015
Cell Culture Techniques Cell Membrane Permeability Cells Culture Media Dielectric Spectroscopy DNA Chips Electric Conductivity Electricity Epithelial Cells Intercellular Junctions Lipid Bilayers Ohmic Resistance Plasma Membrane Tight Junction Proteins

Most recents protocols related to «Tight Junction Proteins»

1
Corneal Epithelial Tissue Processing and Imaging

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Publication 2023
Air Conditioning Cells Cornea Cytokeratin DNA Chips Eosin Epithelial Cells Epithelium, Anterior Corneal Ethanol Hematoxylin Human Body Immunofluorescence Medical Devices Metals Microscopy Paraffin paraform Tight Junction Proteins Tight Junctions Tissue, Membrane Tissues Xylene
2
Neu5Gc Modulates Intestinal Barrier Function
Caco-2 intestinal epithelial cells were purchased from the ATCC (Rockville, MD, USA) and cultivated at 37 °C and 5% CO2 in DMEM medium supplemented with 10% FBS and 1% antibiotics (penicillin/streptomycin). Caco-2 cells were seeded in 6-well plates, 96-well plates, or Transwell polyester membrane inserts and cultivated in a serum-free medium (BIO-MPM-1; BI, Israel) prior to each experiment to eliminate the impact of Neu5Gc in the FBS. The Neu5Gc was dissolved in serum-free culture medium or HBSS solution for the consequent experiment. The toxicity of Neu5Gc was evaluated through the MTT test (described in Section 5.9), and based on the results, a nontoxic concentration of 0.6 mM Neu5Gc was used to examine the mechanism of endocytosis and exocytosis (described in Section 5.6 and Section 5.8). The quantification of Neu5Gc in the Caco-2 cells was conducted by DMB-HPLC (described in Section 5.7). Because ~85% of people consume between 2.92 and 8.76 mmol Neu5Gc per year [16 (link)], and the LC50 value of Neu5Gc (103.9 mM) is extremely high (described in Section 2.3), we choosed 1, 3, and 9 mM Neu5Gc for exploring the Neu5Gc induced damage to intestinal barrier function. Specifically, Caco-2 cells were treated with a solution containing 1, 3, and 9 mM Neu5Gc for 24 h. Then, the TEER (described in Section 5.3) and Papp (described in Section 5.4) of Caco-2 cell monolayers were measured. Subsequently, the inflammatory cytokines and tight-junction proteins mRNA expression (described in Section 5.10), tight-junction proteins and NF-κB related proteins expression (described in Section 5.5 and Section 5.11) were detected. In another experiment, Caco-2 cells were pretreated with BAY, a specific inhibitor of NF-κB signaling pathway, for 2 h, and then incubated with 9 mM Neu5Gc for 24 h, and the related indicators mentioned above were determined.
He E., Quan W., Luo J., Liu C., Zheng W, & Shen Q. (2023). Absorption and Transport Mechanism of Red Meat-Derived N-glycolylneuraminic Acid and Its Damage to Intestinal Barrier Function through the NF-κB Signaling Pathway. Toxins, 15(2), 132.
Publication 2023
1-(2-(4-aminophenyl)ethyl)-4-(3-trifluoromethylphenyl)piperazine Antibiotics Caco-2 Cells Culture Media Cytokine Defecation Endocytosis Exocytosis Hemoglobin, Sickle High-Performance Liquid Chromatographies I-kappa B Proteins Inflammation Intestines Penicillins Polyesters Proteins RELA protein, human RNA, Messenger Serum Signal Transduction Pathways Streptomycin Tight Junction Proteins Tissue, Membrane
3
Evaluating Epithelial Barrier Function
Epithelial barrier function was assessed by evaluating both transepithelial permeability and transepithelial electrical resistance (TEER). To block the action of the ephA2 receptor, ephA2 siRNAs were transfected into cultured epithelial cells or an ephA2 inhibitor (1 μM, ALW-II-41-27, APExBIO, Houston, TX, USA) was added to the culture media for 48 h. Thereafter, cultured cells were treated with ephrinA1 at a dose of 1, 5, 10, and 15 ng/mL or infected with RV for 48 h. Epithelial permeability and TEER were assessed using FITC-dextran (Sigma-Aldrich, St. Louis, MO, USA) and the ERS-2 volt-ohm meter (Millipore, Billerica, MA, USA), respectively. Permeability was analyzed by the application of fluorescein isothiocyanate (FITC)-dextran 4 kDa (Sigma-Aldrich) to the apical surface of cultured cells. Two hours after FITC-dextran was added apically at a concentration of 10 mg/mL, the passage of dextran into the basolateral fluids was analyzed using a Fluoroskan Ascent FL2.5 reader (Thermo Fischer, Loughborough, UK). The concentration of FITC-dextran was expressed as the ratio of the concentration in cells treated with rhinovirus relative to the value for untreated control cells. The values of epithelial permeability and TEER were expressed as a percentage of the control value.
The sinonasal epithelium acts as a protective barrier against pathogens or particles inhaled into the nasal cavities. To manage this task, the nasal epithelial cells comprise tight junctional complexes formed between neighboring cells, including Zonula occludens (ZO)-1, ZO-2, and occludin [2 (link),6 (link)]. To evaluate the effect of the ephrinA1/ephA2 pathway on the expression of tight junctional proteins, the expression and distribution of ZO-1, ZO-2, and occludin (Invitrogen, Waltham, CA, USA) were evaluated by western blotting and confocal microscopy in cultured cells after measurement.
Shin J.M., Han M.S., Park J.H., Lee S.H., Kim T.H, & Lee S.H. (2023). The EphA1 and EphA2 Signaling Modulates the Epithelial Permeability in Human Sinonasal Epithelial Cells and the Rhinovirus Infection Induces Epithelial Barrier Dysfunction via EphA2 Receptor Signaling. International Journal of Molecular Sciences, 24(4), 3629.
Publication 2023
ALW-II-41-27 Cardiac Arrest Cells Cultured Cells Culture Media Dextran Epithelial Cells Epithelium fluorescein isothiocyanate dextran Microscopy, Confocal Nasal Cavity Nose Occludin pathogenesis Permeability Receptor, EphA2 Resistance, Electrical Rhinovirus RNA, Small Interfering SERPINA3 protein, human Tight Junction Proteins Tight Junctions
4
Cytokine and Tight Junction Protein Profiling in Colonic Tissue
All indexes for ELISA were detected from the colonic tissue. The expressions of the cytokines including interferon-γ (IFN-γ), transforming growth factor-β (TGF-β), interleukin (IL)-4, IL-33, IL-13, IL-25, IL-10, tumor necrosis factor-α (TNF-α), and thymicstromal lymphopoietin (TSLP) were determined using by the commercial ELISA kits (eBioscience, San Diego, CA, USA). The level of slgA were also measured by ELISA kit (Bethyl Laboratories, Inc. Montgomery, TX, USA). The concentrations of tight junction proteins including claudin-1, occludin and ZO-1 were detected by the commercial ELISA kits (MyBioSource, San Diego, CA, USA).
Liu P., Zhang M., Liu T., Mo R., Wang H., Zhang G, & Wu Y. (2023). Avenanthramide Improves Colonic Damage Induced by Food Allergies in Mice through Altering Gut Microbiota and Regulating Hsp70-NF-κB Signaling. Nutrients, 15(4), 992.
Publication 2023
Claudin-1 Colon Cytokine Enzyme-Linked Immunosorbent Assay IL33 protein, human Interferon Type II Interleukin-4 Interleukin-10 Interleukin-13 Interleukin-17E Occludin Tight Junction Proteins Tissues Transforming Growth Factors Tumor Necrosis Factor-alpha
5
Gut Microbiota and SCFA Dynamics
All data were analyzed using SPSS v. 22.0 (IBM Corp., Armonk, NY, USA). One-way ANOVA with Duncan’s multiple range test was used to detect cytokine concentrations, tight junction protein levels, SCFAs contents, and the protein gray value among different groups. The Kruskal–Wallis test was conducted to evaluate the abundance of gut microbiota. Spearman Rank analysis was conducted to analyze the association between the abundance of gut microbes and the concentrations of SCFAs. Data are presented as means ± SDs. Statistical significance was decided at p ≤ 0.05.
Liu P., Zhang M., Liu T., Mo R., Wang H., Zhang G, & Wu Y. (2023). Avenanthramide Improves Colonic Damage Induced by Food Allergies in Mice through Altering Gut Microbiota and Regulating Hsp70-NF-κB Signaling. Nutrients, 15(4), 992.
Publication 2023
Cytokine Gastrointestinal Microbiome neuro-oncological ventral antigen 2, human Proteins Tight Junction Proteins

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1
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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.
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Occludin by Abcam
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Occludin is a tight junction protein that plays a crucial role in maintaining the barrier function of epithelial and endothelial cells. It is an integral membrane protein that contributes to the formation and regulation of tight junctions, which are specialized cell-cell adhesion complexes responsible for controlling the movement of molecules across cell layers.
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DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.
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Rabbit anti occludin by Thermo Fisher Scientific
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Rabbit anti-occludin is a primary antibody that specifically binds to the occludin protein. Occludin is a tight junction-associated protein that plays a role in regulating the permeability of epithelial and endothelial cell layers. This antibody can be used for the detection and analysis of occludin in various experimental applications.
8
Rabbit anti zo 1 by Thermo Fisher Scientific
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Rabbit anti-ZO-1 is a primary antibody that specifically binds to the ZO-1 (Zonula Occludens-1) protein. ZO-1 is a tight junction-associated protein that plays a crucial role in the maintenance of cell-cell junctions and the regulation of paracellular permeability. This antibody can be used in various applications such as western blotting, immunohistochemistry, and immunocytochemistry to detect and analyze the expression and localization of the ZO-1 protein.
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Occludin by Thermo Fisher Scientific
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Occludin is a tight junction protein that plays a crucial role in the formation and maintenance of the blood-brain barrier. It is a transmembrane protein involved in cell-cell adhesion and the regulation of paracellular permeability. Occludin is commonly used as a marker for the integrity of tight junctions in various biological and biomedical applications.

More about "Tight Junction Proteins"

Tight Junction Proteins, also known as TJs or Tight Junctions, are a critical component of the cellular junctions that regulate the permeability and transport of molecules across epithelial and endothelial cell layers.
These integral membrane proteins, such as Occludin and Zonula Occludens-1 (ZO-1), play a key role in maintaining tissue integrity, barrier function, and cell-cell communication.
Researchers can leverage powerful tools like PubCompare.ai's AI-powered platform to easily locate, compare, and optimize research protocols for studying Tight Junction Proteins, accelerating their work and improving reproducibility.
This ultimate tool allows users to unlock the best approaches by analyzing protocols from literature, pre-prints, and patents, empowering researchers to advance their understanding of this important class of proteins.
Techniques like TRIzol reagent and RNeasy Mini Kit can be used to extract high-quality RNA from cells, while PrimeScript RT reagent kit and High-Capacity cDNA Reverse Transcription Kit enable efficient reverse transcription.
Antibodies such as Rabbit anti-occludin and Rabbit anti-ZO-1 can be employed for immunodetection, and the BCA protein assay kit can be utilized to quantify protein levels.
By incorporating these tools and methodologies, researchers can gain deeper insights into the structure, function, and regulation of Tight Junction Proteins, ultimately contributing to our understanding of epithelial and endothelial barrier function in health and disease.