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Galactose Binding Lectin

Galactose Binding Lectin is a type of carbohydrate-binding protein that specifically recognizes and binds to galactose and galactose-containing molecules.
These lectins play crucial roles in various biological processes, including cell-cell interactions, cell adhesion, and immune response.
Researchers can explore the power of Galactose Binding Lectin research using PubCompare.ai's AI-driven platform, which provides access to protocols from literature, preprints, and patents.
The platform's intelligent comparisons can help identify the optimal techniques and products for your research, streamlining your workflow and accelerating discoveries with cutting-edge technology.

Most cited protocols related to «Galactose Binding Lectin»

Placental Gene Regulation and Trophoblast Function

Cited 7 times

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Publication 2014

5' Untranslated Regions Anti-Antibodies Antibodies Binding Sites Biological Assay Biological Evolution Biopharmaceuticals CEBPB protein, human Cells DNA Chips DNA Transposable Elements Exons Formalin Freezing Galactose Binding Lectin Genes Genome Homo sapiens hydrogen sulfite Immunoprecipitation In Situ Hybridization isolation Laser Capture Microdissection LGALS13 protein, human Luciferases Methylation Microarray Analysis N-tris(hydroxymethyl)methyl-2-aminomethane sulfonate Paraffin Placenta Pseudogenes Specimen Collection Tissues Transcription, Genetic Transcription Factor Trees Trophoblast Umbilical Cord Blood Untranslated Regions Woman

Cryo-EM structure determination of SARS-CoV-2 spike protein

Cited 4 times

Fitting of atomic models into cryoEM maps was performed using UCSF Chimera^{45 (link)} and Coot^{18 (link),46 (link)}. We initially docked the MHV domain A structure (PDB 3R4D) and used a crystal structure of a bovine coronavirus domain A (PDB 4H14) to model the three-stranded β-sheet and the α-helix present on the viral membrane proximal side of the galectin-like domain. Next, the MERS-CoV domain B crystal structure (PDB 4KQZ) was also fit into the density, and rebuilt and refined using RosettaCM^{47 (link)}. Although we could accurately align the sequences corresponding to the core β-sheet of the MHV and MERS-CoV B domains, the ~100 residues forming the β-motif extension (residues 453-535, MERS-CoV/SARS-CoV receptor-binding moiety) could not be aligned with confidence. We used RosettaCM to build models of each of the 945 possible disulfide patterns into the density for domain B. For each disulfide arrangement, 50 models were generated, and there was a very clear energy signal for a single such arrangement (ED Fig.3k). Then, 1000 models with this disulfide arrangement were sampled, and the lowest energy model (using the Rosetta force field augmented with a fit-to-density score term) was selected. Due to the poor quality of the reconstruction at the apex of the S trimer, the confidence of the model is lowest for the segment corresponding to residues 453-535, as homology-modeling was used to fill in details missing in the map.
A backbone model was then manually built for the rest of the S polypeptide using Coot. Sequence register was assigned by visual inspection where side chain density was clearly visible. This initial hand built model was used as an initial model for Rosetta de novo^{20 (link)}. The Rosetta-derived model largely agreed with the hand-built model. Rosetta de novo successfully identified fragments allowing to anchor the sequence register for domains C and D as well as for helices α₂₁-α₂₅. Given these anchoring positions, RosettaCM^{47 (link)} augmented with a novel density-guided model-growing protocol was able to rebuild domains C and D in full. The final model was refined by applying strict non-crystallographic symmetry constraints using Rosetta^{19 (link)}. Model refinement was performed using a training map corresponding to one of the two maps generated by the gold-standard refinement procedure in Relion. The second map (testing map) was used only for calculation of the FSC compared to the atomic model and preventing overfitting^{48 (link)}. The quality of the final model was analyzed with Molprobity^{49 (link)}. Structure analysis was assisted by the PISA^{50 (link)} and DALI^{51 (link)} servers. The sequence alignment was generated using MultAlin^{52 (link)} and colored with ESPript^{53 (link)}. All figures were generated with UCSF Chimera^{45 (link)}.

Walls A.C., Tortorici M.A., Bosch B.J., Frenz B., Rottier P.J., DiMaio F., Rey F.A, & Veesler D. (2016). Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature, 531(7592), 114-117.

Publication 2016

Coronavirus, Bovine Cryoelectron Microscopy Crystallography Disulfides Galactose Binding Lectin Gold Helix (Snails) Microtubule-Associated Proteins Middle East Respiratory Syndrome Coronavirus Polypeptides Reconstructive Surgical Procedures Sequence Alignment Severe acute respiratory syndrome-related coronavirus Tissue, Membrane Vertebral Column

Glycan Microarray Binding Assay

Cited 4 times

The Consortium for Functional Glycomics (http://www.functionalglycomics.org/) provided glycan microarrays (v4.2) prepared as described previously ^{45 (link),47 (link)}. For galectin recognition of glycans on the printed glycan microarray, slides were incubated with 0.2 µM or 5 µM Gal-4, or 5 µM Gal-8 in TSM binding buffer + 14 mM 2-ME for 1h at room temperature in a dark humid chamber. The slide was washed by successive immersion in TSM containing 0.05% Tween 20 (4 times) and TSM (4 times). The slide was incubated with Alexa Fluor-488-streptavidin. After 1h at room temperature in a dark humid chamber, we washed the slide by successive immersion in TSM containing 0.05% Tween 20 (4 times), TSM (4 times), and water (4 times). The slide was dried by microcentrifugation and an image of bound fluorescence was obtained using a microarray scanner (Scan Array Express, PerkinElmer Lifer Sciences). Integrated spot intensities were determined using Imagene software (BioDiscovery).

Stowell S.R., Arthur C.M., McBride R., Berger O., Razi N., Heimburg-Molinaro J., Rodrigues L.C., Gourdine J.P., Noll A.J., von Gunten S., Smith D.F., Knirel Y.A., Paulson J.C, & Cummings R.D. (2014). Microbial Glycan Microarrays Define Key Features of Host-Microbial Interactions. Nature chemical biology, 10(6), 470-476.

Publication 2014

alexa fluor 488 Buffers Fluorescence Galactose Binding Lectin LGALS8 protein, human Microarray Analysis Polysaccharides Radionuclide Imaging Streptavidin Submersion Tween 20

Recombinant Galectin-3 Purification and Analysis

Cited 4 times

Recombinant human galectin-3 and mutants and Xenopus galectin-3 were produced in E. coli BL21Star (DE3) cells (Invitrogen) and purified by affinity chromatography on lactosyl-Sepharose essentially as described for wild type human galectin-3 (34 (link)) but with some variation to optimize yield for each protein. The initial yields ranged from 3 mg/liter culture for G182A to 80 mg/liter for R144S, but, for example, lowering the temperature of the isopropyl 1-thio-β-d-galactopyranoside induction from 37 to 30 °C increased the yield of G182A galectin-3 about 10-fold. Mouse galectin-3 was produced from vector pIN III ompA2 in E. coli JA221 cells as previously described (36 (link)), except that Tryptone soy broth was used. The bacteria were processed and galectin-purified in the same way as for human galectin-3 described above. The galectins, in phosphate-buffered saline (118 mm NaCl, 67 mm Na⁺/K⁺-phosphate, pH 7.2) containing 4 mm β-mercaptoethanol, 2 mm EDTA and 150 mm lactose, were dialyzed against 2 liters of water that was changed once every 2 h 7 times and lyophilized and stored at −20 °C until use. This procedure does not completely deplete the galectin-bound lactose, which helps to preserve stability. Before use, the galectins were dissolved in the appropriate buffer, and any remaining lactose was removed by repeated ultrafiltration and concentration in a Centricon Plus-70, Ultracel PL10, or Centriprep Y10 ultrafiltration cell (Millipore AB, Sundbyberg, Sweden). Protein concentrations were determined using the Bio-Rad protein assay (Bio-Rad, Sundbyberg, Sweden). Protein size and integrity was determined by SDS-PAGE using 4–20% Precise^TM Protein Gels from Pierce (Nordic Biolabs, Täby, Sweden) in Tris/HEPES running buffer.
Differential scanning calorimetry measurements were performed on a MicroCal differential scanning calorimeter (MicroCal Inc., Northampton, MA) with a cell volume of 0.5072 ml. All samples were degassed for 15 min at room temperature before scanning. Protein samples (0.5 mg/ml) in PBS buffer with or without ligand were scanned in the temperature range 25 to 80 °C at a rate of 1 °C/min.The reversibility of the calorimetric traces was assessed by the reproducibility of scans upon rapid cooling to 25 °C followed by rescanning. Base-line scans were collected with buffer in both the reference and sample cells.

Salomonsson E., Carlsson M.C., Osla V., Hendus-Altenburger R., Kahl-Knutson B., Öberg C.T., Sundin A., Nilsson R., Nordberg-Karlsson E., Nilsson U.J., Karlsson A., Rini J.M, & Leffler H. (2010). Mutational Tuning of Galectin-3 Specificity and Biological Function. The Journal of Biological Chemistry, 285(45), 35079-35091.

Publication 2010

2-Mercaptoethanol Bacteria BaseLine dental cement Biological Assay Buffers Calorimetry Calorimetry, Differential Scanning Cells Chromatography, Affinity Cloning Vectors Edetic Acid Escherichia coli Galactose Galactose Binding Lectin Galectin 3 Gels HEPES Lactose LGALS3 protein, human Ligands Mus Phosphates Proteins Radionuclide Imaging Saline Solution SDS-PAGE Sepharose Sodium Chloride Tromethamine Ultrafiltration Xenopus laevis

Evaluating Gal-3 Binding to Neo-Glycoproteins

Cited 3 times

The affinity of Gal-3 for neo-glycoproteins 9–16 was determined using ELISA as reported previously [15 (link),27 (link),30 (link),49 (link)]. For the immobilization of the respective neo-glycoproteins or non-modified BSA (negative control), we used F16 Maxisorp NUNC-Immuno Modules (Thermo Scientific, Roskilde, Denmark). Per well, an amount of 5 pmol was incubated overnight at a working concentration of 0.1 µM (PBS). Then the wells were blocked with bovine serum albumin (2% w/v) diluted in PBS (1 h, room temperature). Afterwards, recombinant Gal-3 in varying concentration (total volume 50 µL) was added and incubated for 1 h. Detection of bound Gal-3 was achieved using anti-His₆-IgG1 antibody from mouse conjugated with horseradish peroxidase (Roche Diagnostics, Mannheim, Germany) diluted in PBS (1:2000, 50 µL, 1 h, room temperature). TMB One (Kem-En-Tec, Taastrup, Denmark) substrate solution was utilized to initiate reaction of IgG-conjugated peroxidase. The reaction was stopped by adding 3 M hydrochloric acid (50 µL). The binding signal of bound galectin was measured with a spectrophotometer (Spectra Max Plus, Molecular Devices, Sunnyvale, CA, USA) at an optical density of 450 nm. Obtained data were analyzed using SigmaPlot 10 software (Systat Software GmbH, Erkrath, Germany).
In the competitive ELISA design, the F16 Maxisorp NUNC-Immuno Modules (Thermo Scientific, Roskilde, Denmark) were coated overnight with ASF (Sigma Aldrich, Steinheim, Germany; 0.1 µM in PBS, 50 µL, 5 pmol per well) and blocked with BSA (2% w/v) diluted in PBS (1 h, room temperature). Afterwards, a mixture of the respective compound 1–16 in varying concentrations together with Gal-3 (total volume 50 µL; 5 µM final Gal-3 concentration) were added and incubated for 1 h. Detection of bound Gal-3 and data analysis were performed as described above.

Bumba L., Laaf D., Spiwok V., Elling L., Křen V, & Bojarová P. (2018). Poly-N-Acetyllactosamine Neo-Glycoproteins as Nanomolar Ligands of Human Galectin-3: Binding Kinetics and Modeling. International Journal of Molecular Sciences, 19(2), 372.

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Publication 2018

Antibodies, Anti-Idiotypic Diagnosis Enzyme-Linked Immunosorbent Assay fluoromethyl 2,2-difluoro-1-(trifluoromethyl)vinyl ether Galactose Binding Lectin Glycoproteins Horseradish Peroxidase Hydrochloric acid IgG1 Immobilization LGALS3 protein, human Medical Devices Mice, House Peroxidase Serum Albumin, Bovine

Most recents protocols related to «Galactose Binding Lectin»

Quantifying Bone Resorption Using Osteoclasts

For bone resorption assays, BMDMs or pre-osteoclasts were seeded and cultured on bovine cortical bone slices (DT-1BON1000-96; Immunodiagnostic Systems) with 20 ng/ml M-CSF and 30 ng/ml RANKL (R&D Systems; Wu et al., 2017 (link); Zhang et al., 2018 (link); Zhu et al., 2020 (link)), in the presence or absence of galectin-3 (8259-GA; R&D Systems), galectin-3C (10110-GA; R&D Systems), GCS-100 (La Jolla Pharmaceutical), RAP (4480-LR; R&D Systems), an anti–galectin-3 blocking antibody (sc-32790L; Santa Cruz), or an anti-Lrp1 blocking antibody (MA1-27198; Thermo Fisher Scientific; Chen et al., 2015 (link); Demotte et al., 2010 (link); John et al., 2003 (link); Moxon et al., 2015 (link); Seguin et al., 2017 (link)). After the indicated culture period, bone samples were sonicated in PBS, stained with 20 μg/ml WGA-lectin (L3892; Sigma-Aldrich) for 45 min and then incubated with DAB tablets (D4418; Sigma-Aldrich) for 15 min. Image J software was used to quantify the resorbed area. The concentration of the CTX-I was measured using the CrossLaps for Culture CTX-I ELISA kit (AC-07F1; Immunodiagnostic Systems) according to the manufacturer’s instructions.

Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.

Publication 2023

Antibodies, Anti-Idiotypic Antibodies, Blocking Biological Assay Bone Resorption Bones Bos taurus Cardiac Arrest Compact Bone Enzyme-Linked Immunosorbent Assay Galactose Binding Lectin Galectin 3 GCS-100 glutamyl-lysyl-alanyl-histidyl-aspartyl-glycyl-glycyl-arginine Immunodiagnosis Lectin Macrophage Colony-Stimulating Factor Osteoclasts Pharmaceutical Preparations Physiotens TNFSF11 protein, human

Osteoclast Galectin Expression Profiling

Single-cell suspensions of osteoclasts were collected after passing through a 40 µm cell strainer (BD Bioscience), incubated with Fc receptor block (#101319; Biolegend) for 10 min, and then incubated with CoraLite 488–conjugated galectin-3 polyclonal antibody (rabbit anti-mouse antibody; CL488-14979; Proteintech; epitopes mapped throughout the full-length protein), eFluor 660–conjugated anti–galectin-3 monoclonal antibody (rabbit anti-mouse antibody; #50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal region), PE-conjugated anti–galectin-1 antibody (goat anti-mouse antibody; IC1245P; R&D), or the corresponding rabbit and goat isotype control (#31235; #31245; Invitrogen) in flow cytometry staining buffer (eBioscience) for 30 min at 4°C. For Mitotracker Green staining, cells were incubated with 100 nM Mitotracker Green (M7514; Invitrogen) in HBSS for 45 min. Then, cells were subjected to flow cytometry analysis on a FACS Canto II (BD Bioscience). Data analysis was carried out using FlowJo software.

Publication 2023

Antibodies, Anti-Idiotypic Buffers Cells Clone Cells Epitopes Fc Receptor Flow Cytometry Galactose Binding Lectin Galectin 3 Goat Hemoglobin, Sickle Immunoglobulin Isotypes Immunoglobulins LGALS1 protein, human Mus Osteoclasts Proteins Rabbits

Multiparametric Immunophenotyping of Tumor Microenvironment

Thermo Fisher Scientific supplied mouse anti-E-cadherin, mouse anti-vimentin, mouse anti-catenin, mouse anti-galectin, mouse anti-PD-L1, mouse anti-TGF, mouse anti-NF-κB antibodies, mouse anti-STAT3, and Hoechst (Waltham, MA, USA). eBio-science provided mouse anti-CD163-PerCP, mouse anti-CD206-PerCP, mouse anti-Ki-67-APC, mouse anti-CD68-FITC, and mouse anti-IL-10-FITC (San Diego, CA, USA). BD Cytofix/Cytoperm Fixation/Permeabilization Solution Kit with GolgiPlug™(No. BDB555028, San Diego, CA, USA). PeproTech delivered recombinant mouse IL-4, IFN-, and anti-IL-10 receptor (abIL-10R) inhibitors (Rocky Hill, NJ, USA).
mouse anti-STAT3 (Invitrogen, cat number MA1-13042), rabbit anti-NF-κB (Life technologies, cat number 510500), mouse anti-PD-L1/CD274 (Proteintech, cat number 66248-1-Ig), and mouse anti-TGF (Invitrogen, cat number MA5-15065) were used for immunoblotting, and so were secondary antibodies goat anti-mouse and goat anti-rabbit Alexa® Fluor 555 (Thermo Fisher Scientific, Waltham). For immunoblotting, rabbit anti-actin (LI-COR Biosciences, Lincoln, Nebraska, USA) was used. The anti-mouse PD-L1 checkpoint blocker was purchased from InVivoPlus (B7-H1, Bio cell, USA).

Júnior R.F., Lira G.A., Schomann T., Cavalcante R.S., Vilar N.F., de Paula R.C., Gomes R.F., Chung C.K., Jorquera-Cordero C., Vepris O., Chan A.B, & Cruz L.J. (2023). Retinoic acid-loaded PLGA nanocarriers targeting cell cholesterol potentialize the antitumour effect of PD-L1 antibody by preventing epithelial-mesenchymal transition mediated by M2-TAM in colorectal cancer. Translational Oncology, 31, 101647.

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Publication 2023

Actins Alexa Fluor 555 Anti-Antibodies Antibodies Cadherins Catenins CD163 protein, human CD274 protein, human Cell Cycle Checkpoints Cells Fluorescein-5-isothiocyanate Galactose Binding Lectin GIT1 protein, human Goat IL10 protein, human Interleukin Inhibitors Mus Rabbits RELA protein, human STAT3 Protein Vimentin

Live Imaging of siRNA Delivery and Intracellular Dynamics

HeLa cells stably expressing d1-eGFP or YFP-galectin-9 or transiently expressing GFP-AGO2 were plated in microscopy slides as described. Cells were transferred to a preheated microscopy incubation chamber, and 4–6 positions with sparse and evenly distributed cells were selected. Immediately before starting image acquisition, lipoplexes formulated with siGFP-1, siGFP-2, siLuc, or siRNA-AF647(as) were added dropwise to the medium. Typically, 5 or 10 µL of the siRNA-lipoplex solution was added to the well. For d1-eGFP knockdown experiments, one well was left untreated as a control and imaged using the same settings as treated cells. Two z-plane images with 4 µm z-spacing were acquired per position at 5 min intervals. The lower z-plane was set in the lower third of the cells (see confocal microscopy section for details). AF647-siRNA fluorescence was detected with an Airyscan detector while Hoechst 33342 and d1-eGFP fluorescence was detected with a PMT detector. Typically, images were acquired for 12–32 h for knockdown experiments and 6–8 h for galectin-9 recruitment experiments. AF647-siRNA bleaching was quantified in non-internalized glass-adhering lipoplexes.
For high-temporal resolution imaging of cytosolic siRNA release, a single z-plane set in the lower third of the cell was acquired at 5 s intervals (single position) and typically imaged for 25 min.

Hedlund H., Du Rietz H., Johansson J.M., Eriksson H.C., Zedan W., Huang L., Wallin J, & Wittrup A. (2023). Single-cell quantification and dose-response of cytosolic siRNA delivery. Nature Communications, 14, 1075.

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Publication 2023

Alexa Fluor 647 Cytosol EIF2C2 protein, human Fluorescence Galactose Binding Lectin HeLa Cells HOE 33342 LGALS9 protein, human Microscopy Microscopy, Confocal RNA, Small Interfering

Oligomerization Analysis of Gal-3 Constructs

To investigate the oligomerization of different Gal-3 constructs, a Superdex 200 Increase 10/300 GL column (Cytiva, Dreieich, Germany) was used. The maximum pressure limit of the column was determined by Equations (1)–(3).

pmax = Δ p + Δ pafter + Δ pbefore

Δ p = Δ pcolumn - Δ pbefore

Δ pafter = Δ ptotal - Δ pbefore(2)

Linear regression was used to calculate the molecular weights of galectin samples. For this, the K_AV (Equation (4)) of Blue Dextran and protein standards (High Molecular Weight and Low Molecular Weight; Cytiva, Germany) were plotted over the logarithmic molecular weights of the standard proteins (Figure S13). The elution volume of the samples was determined by applying 200 µL galectin sample (sterile filtered, 0.2 µM) to the column via loop injection at a constant flow rate of 0.75 mL x min⁻¹ with PBS pH 7.5 as running buffer. The elution was monitored at 280 nm.

K_{AV} [-] = \frac{V_{e} - V_{o}}{V_{c} - V_{0}}

Dey C., Palm P, & Elling L. (2023). Characterization of Galectin Fusion Proteins with Glycoprotein Affinity Columns and Binding Assays. Molecules, 28(3), 1054.

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Publication 2023

blue dextran Buffers Galactose Binding Lectin LGALS3 protein, human Pressure Proteins Sterility, Reproductive X-Flow

Top products related to «Galactose Binding Lectin»

Galectin 3 by R&D Systems

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Galectin-3 is a mammalian lectin protein that binds to beta-galactoside sugars. It plays a role in various biological processes, including cell-cell adhesion, cell-matrix interactions, and immune regulation.

96 well tissue plates by Greiner

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The 96-well tissue plates are a laboratory equipment designed for cell culture applications. They provide a standardized multi-well format for seeding and growing cells. The plates have a flat bottom and are made of tissue culture-treated polystyrene to support cell attachment and proliferation.

Peaq itc calorimeter by Malvern Panalytical

Sourced in United States

The PEAQ-ITC calorimeter is a laboratory instrument designed for isothermal titration calorimetry (ITC) measurements. ITC is a technique used to study molecular interactions, thermodynamics, and binding affinities between various biomolecules, such as proteins, nucleic acids, and small molecules. The PEAQ-ITC calorimeter measures the heat changes that occur during these interactions, providing detailed information about the thermodynamic properties of the system under investigation.

Fetal calf serum (fcs) by Thermo Fisher Scientific

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Fetal calf serum is a nutrient-rich cell culture supplement derived from the blood of bovine fetuses. It provides a complex mixture of proteins, growth factors, and other components that support the growth and proliferation of cells in in vitro cell culture systems.

Pd 10 column by GE Healthcare

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The PD-10 column is a size-exclusion chromatography column designed for desalting and buffer exchange of protein samples. It is commonly used to separate low molecular weight substances from high molecular weight compounds, such as proteins, in a rapid and efficient manner.

Lipofectamine 2000 by Thermo Fisher Scientific

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Muc1 aa1 264 by OriGene

MUC1 (aa1-264) is a recombinant protein product that represents the extracellular domain of the human MUC1 protein, encompassing amino acids 1 to 264. MUC1 is a transmembrane glycoprotein that plays a role in cell-cell and cell-matrix interactions.

Muc16 aa21005 21992 by R&D Systems

MUC16 (aa21005-21992) is a recombinant protein product from R&D Systems. It represents a partial sequence of the MUC16 protein, encompassing amino acids 21005 to 21992.

Tween 20 by Merck Group

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Tween 20 is a non-ionic detergent commonly used in biochemical applications. It is a polyoxyethylene sorbitan monolaurate, a surfactant that can be used to solubilize and stabilize proteins and other biomolecules. Tween 20 is widely used in various laboratory techniques, such as Western blotting, ELISA, and immunoprecipitation, to prevent non-specific binding and improve the efficiency of these assays.

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Lipofectamine 3000 is a transfection reagent used for the efficient delivery of nucleic acids, such as plasmid DNA, siRNA, and mRNA, into a variety of mammalian cell types. It facilitates the entry of these molecules into the cells, enabling their expression or silencing.

What are the different types or variations of Galactose Binding Lectin?

Galactose Binding Lectins can be classified into several types based on their structural and functional characteristics. Some common variations include C-type lectins, which require calcium for carbohydrate binding, and galectins, which are a family of beta-galactoside-binding proteins. These different types of Galactose Binding Lectins can exhibit distinct binding specificities and play diverse roles in biological processes.

What are the key applications of Galactose Binding Lectin research?

Galactose Binding Lectins have a wide range of applications in various fields, including cell biology, immunology, and diagnostics. Researchers often use these lectins to study cell-cell interactions, cell adhesion, and immune responses. They can also be employed as tools for glycan profiling, cell labeling, and affinity purification of glycoproteins. Additionally, Galactose Binding Lectin research has implications in the development of therapeutic interventions, such as anti-cancer therapies and targeted drug delivery.

What are some common challenges in working with Galactose Binding Lectin?

One of the main challenges in Galactose Binding Lectin research is the potential for non-specific binding, which can lead to false positive results or interference with experimental observations. Researchers must carefully optimize experimental conditions, such as lectin concentration, incubation time, and buffer composition, to minimize non-specific interactions. Additionally, the diversity of Galactose Binding Lectin types and their varying binding specificities can complicate the selection of the appropriate lectin for a particular application.

How can PubCompare.ai assist in Galactose Binding Lectin research?

PubCompare.ai's AI-driven platform can be a valuable tool for Galactose Binding Lectin researchers. The platform allows you to efficiently screen protocol literature, including publications, preprints, and patents, to identify the most effective techniques and products for your specific research goals. PubCompare.ai's intelligent comparisons can help you pinpoimt key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy. This can streamline your workflow and accelerate your discoveries with cutting-edge technology.

Can PubCompare.ai help identify the optimal Galactose Binding Lectin for my research?

Absolutely! PubCompare.ai's AI-driven analysis can help you identify the most appropriate Galactose Binding Lectin for your research. By leveraging the platform's extensive protocol data, the AI can highlight the key differences in lectin binding specificity, performance, and suitability for your experimental setup. This can assist you in selecting the optimal Galactose Binding Lectin variant that will provide the most accurate and reliable results, ultimately enhancing the quality and efficiency of your research.

More about "Galactose Binding Lectin"

Galactose-binding lectins, also known as galectins, are a family of carbohydrate-binding proteins that specifically recognize and bind to galactose and galactose-containing molecules.
These proteins play crucial roles in a wide range of biological processes, including cell-cell interactions, cell adhesion, and immune response.
Researchers can explore the power of galectin research using PubCompare.ai's AI-driven platform, which provides access to protocols from literature, preprints, and patents.
The platform's intelligent comparisons can help identify the optimal techniques and products for your research, streamlining your workflow and accelerating discoveries with cutting-edge technology.
Galectin-3, a member of the galectin family, is a multifunctional protein that has been implicated in various cellular processes, such as cell growth, differentiation, and apoptosis.
It is often used in research alongside Galactose Binding Lectin to study carbohydrate-protein interactions.
In addition to galectins, researchers may utilize 96-well tissue plates, PEAQ-ITC calorimeters, and fetal calf serum to conduct their experiments.
PD-10 columns can be used for protein purification, while Lipofectamine 2000 and Lipofectamine 3000 are transfection reagents commonly used to introduce genetic material into cells.
Mucin proteins, such as MUC1 and MUC16, are also relevant to Galactose Binding Lectin research, as they contain carbohydrate moieties that can interact with these lectins.
Tween 20 is a detergent often used in various experimental protocols to reduce non-specific binding and improve assay performance.
By incorporating these related terms, abbreviations, and key subtopics, researchers can gain a more comprehensive understanding of the field of Galactose Binding Lectin research and leverage the powerful tools and techniques available to accelerate their discoveries.