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Galectin 3

Galectin 3 is a beta-galactoside-binding lectin that plays a role in various biological processes, including cell growth, differentiation, and apoptosis.
It has been implicated in the pathogenesis of various diseases, such as cancer, fibrosis, and inflammation.
Galectin 3 is expressed in a variety of cell types and can be found both intracellularly and extracellularly.
Its functions are mediated through binding to specific carbohydrate moieties on cell surface glycoproteins and glycolipids.
Researchers can leverage PubCompare.ai, an AI-powered platform, to enhance their Galectin 3 research by locating protocols from literature, pre-prints, and patents, and utilizing AI-driven comparisons to identify the best protocols and prodducts for their studies, helping to optimize reproducibility and accuracy.

Most cited protocols related to «Galectin 3»

1
Immunofluorescent Analysis of Brachiocephalic Artery Lesions
Cited 9 times
Paraffin-embedded brachiocephalic arteries (BCAs) were serially
sectioned at 10 μm thickness from the aortic arch to the right subclavian
artery. For immunofluorescent analysis of LGALS3+ SMCs within the,
BCA three sections were taken 300 μm apart, spanning the length of the
BCA. Slides were stained with antibodies to GFP (Abcam ab6673), ACTA2 (Sigma
F3777), LGALS3 (Cedarlane CL8942AP), MKI67 (Abcam ab15580), CASP3 (Cell
Signaling 9661S), KLF4 (R&D Systems AF3158), MYH11 (Kamiya Biomedical
Company MC-352), PDGFβR (Abcam ab32570), and SCA1 (Ly6A/E) (Abcam
ab51317). Using a Zeiss LSM700 confocal microscope a series of 8 z-stack images
of 1 μm thickness were acquired for further analysis. Five 14283
μm2 locations within each z-stack of every BCA were
analyzed using Zen 2009 Light Edition Software for the presence of
immunofluorescent staining coinciding with a single DAPI+ nucleus to
determine the average cell populations within each lesion. Every plane of the
z-stack was used to assess the co-localization of cellular markers within a
single cell. The region of the lesion within 30 μm of the luminal
boundary, as determined using Zen 2009 Light Edition Software, was analyzed to
determine the cellular composition of the lesion cap, the area within this
region was compared to the entire area of the atherosclerotic lesion to
determine cap area/lesion area. Morphometric analyses of lesion size were
completed using ImagePro Plus as described in Alexander et
al61 (link).
Researchers were blinded to the genotype of the animals until the end of the
analysis.
Shankman L.S., Gomez D., Cherepanova O.A., Salmon M., Alencar G.F., Haskins R.M., Swiatlowska P., Newman A.A., Greene E.S., Straub A.C., Isakson B., Randolph G.J, & Owens G.K. (2015). KLF4 Dependent Phenotypic Modulation of SMCs Plays a Key Role in Atherosclerotic Plaque Pathogenesis. Nature medicine, 21(6), 628-637.
Publication 2015
ACTA2 protein, human Animals Antibodies Arch of the Aorta CASP3 protein, human Caspase 3 Cells DAPI Fluorescent Antibody Technique Galectin 3 Genotype KLF4 protein, human Light MC 352 Microscopy, Confocal MKI67 protein, human Nucleus Solitarius Paraffin Population Group Trunks, Brachiocephalic
2
Galectin-3 CRD Expression and Purification
Cited 9 times
The galectin-3 CRD (Gal3C; amino acid residues 113−250) was expressed and purified as either a thioredoxin fusion construct(25 (link)) or isolated Gal3C. The expression protocol was identical for the two constructs and has been reported elsewhere.(25 (link)) The purification protocol for isolated Gal3C was very similar to that reported previously,25 (link),64 (link) except that the final steps including and following cleavage were omitted. 15N/13C/2H-labeled Gal3C was expressed in 60% D2O using published protocols.(65 (link)) To obtain stereospecific methyl assignments, one culture was grown on a mixture of 10% uniformly 13C-labeled and 90% unlabeled glucose.(66 (link)) Typical yields of isolated Gal3C were 100−150 mg/L of culture.
Diehl C., Engström O., Delaine T., Håkansson M., Genheden S., Modig K., Leffler H., Ryde U., Nilsson U.J, & Akke M. (2010). Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3. Journal of the American Chemical Society, 132(41), 14577-14589.
Publication 2010
Amino Acids Cytokinesis Galectin 3 Glucose isolation & purification TXN protein, human
3
Chromatin Immunoprecipitation Assay Protocol
Cited 7 times
Chromatin immunoprecipitation assays were performed essentially as described before (Li et al., 2017 (link), 2018c (link),d (link), 2019b (link); Yu et al., 2017 (link), 2018 (link); Fan et al., 2019 (link); Kong et al., 2019a (link), b ; Liu et al., 2019b (link); Weng et al., 2019 (link); Yang et al., 2019a (link), b (link); Zhang et al., 2019 (link)). In brief, chromatin in control and treated cells were cross-linked with 1% formaldehyde. Cells were incubated in lysis buffer (150 mM NaCl, 25 mM Tris pH 7.5, 1% Triton X-100, 0.1% SDS, 0.5% deoxycholate) supplemented with protease inhibitor tablet and PMSF. DNA was fragmented into ∼500 bp pieces using a Branson 250 sonicator. Aliquots of lysates containing 200 μg of protein were used for each immunoprecipitation reaction with the following antibodies: anti-Brg1 (Santa Cruz, sc-17796), anti-acetyl histone H3 (Millipore, 06-599), anti-trimethyl H3K4 (Millipore, 07-473), anti-dimethyl H3K9 (Millipore, 07-441), anti-5′-hydroxymethylcytosine (Abcam, ab106918), anti-5′-methylcytosine (Abcam, ab10805), anti-TET1 (Active Motif, 61443), anti-TET2 (Millipore, MABE462), anti-TET3 (ABE290), anti-c-Jun (Santa Cruz, sc-1694), anti-c-Fos (Santa Cruz, sc-52), or IgG. Precipitated DNA was amplified with the following primers: for LGALS3 promoter (-402/-73), 5′-AATTTGTAGTCAGTTCCCTAG-3′ and 5′-AAATACTCCCAGCCCCGC-3; for LGALS3 promoter (-1276/-959), 5′-ATACCTGGTTTTCTCCATAG-3′ and 5′-ATATTGCCTATAAGCTACCC-3′.
Li Z., Lv F., Dai C., Wang Q., Jiang C., Fang M, & Xu Y. (2019). Activation of Galectin-3 (LGALS3) Transcription by Injurious Stimuli in the Liver Is Commonly Mediated by BRG1. Frontiers in Cell and Developmental Biology, 7, 310.
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Publication 2019
Antibodies Biological Assay Buffers Cells Chromatin Deoxycholate Formaldehyde Galectin 3 Histone H3 Immunoprecipitation Immunoprecipitation, Chromatin Oligonucleotide Primers Protease Inhibitors Proteins SMARCA4 protein, human Sodium Chloride Tablet Triton X-100 Tromethamine
4
Comprehensive Liver Analyses in NAFLD
Cited 7 times
Biochemical and histological analyses were performed as reported previously[19 (link)]. Plasma analytes included alanine aminotransferase (ALT), aspartate aminotransferase (AST), triglycerides (TG) and total cholesterol (TC). Liver homogenates were analyzed for TG and TC. Paraformaldehyde-fixed liver pre- and post-biopsies were paraffin-embedded, sectioned, and stained with hematoxylin-eosin (Dako, Glostrup, Denmark), Picro-Sirius red (Sigma-Aldrich, Broendby, Denmark), anti-type I collagen (Col1a1; Southern Biotech, Birmingham, AL), or anti-galectin-3 (Biolegend, San Diego, CA, United States). The NAFLD activity score (NAS) and fibrosis staging system was applied to liver pre-biopies and terminal samples (drug treatment experiments) or only terminal samples (disease progression experiment) for scoring of steatosis, lobular inflammation, hepatocyte ballooning, and fibrosis outlined by Kleiner et al[31 (link)]. All histological assessments were performed by a pathologist blind to treatment. Because all treatment paradigms affected total liver weight, quantitative data on liver biochemistry (liver TG, TC) and histology (liver lipid, galectin-3, Col1a1) were expressed as whole-liver amounts by multiplying individual terminal liver weight with the corresponding liver lipid concentration (biochemistry data) or percent fractional area (histology data), respectively.
Tølbøl K.S., Kristiansen M.N., Hansen H.H., Veidal S.S., Rigbolt K.T., Gillum M.P., Jelsing J., Vrang N, & Feigh M. (2018). Metabolic and hepatic effects of liraglutide, obeticholic acid and elafibranor in diet-induced obese mouse models of biopsy-confirmed nonalcoholic steatohepatitis. World Journal of Gastroenterology, 24(2), 179-194.
Publication 2018
Aspartate Transaminase Biopsy Blindness Cholesterol Collagen Type I D-Alanine Transaminase Disease Progression Eosin Fibrosis Galectin 3 Hepatocyte Inflammation Lipids Liver Non-alcoholic Fatty Liver Disease Paraffin paraform Pathologists Pharmaceutical Preparations Plasma Steatohepatitis Triglycerides
5
Histological Assessment of Kidney Injury
Cited 6 times
Kidneys were rapidly removed from each mouse and then fixed in 4% phosphate-buffered paraformaldehyde. The tissues were embedded in paraffin and then thin sections were made from the paraffin blocks. The sections were incubated with hematoxylin and eosin (H&E) stain and periodic acid Schiff (PAS) stain. Images were captured using the NIKON A1+ confocal microscope (Nikon, Tokyo, Japan). The degree of tubular injury was scored as previously described [18 (link)]. For immunohistochemical staining, the kidney sections were probed with antibodies against kidney injury molecule-1 (Kim-1; Abcam, Cambridge, MA, USA), neutrophil gelatinase-associated lipocalin (NGAL; Santa Cruz Biotechnology), 4-hydroxynonenal (4-HNE; Abcam), or Galectin-3 (Abcam).
Kim J.Y., Jo J., Kim K., An H.J., Gwon M.G., Gu H., Kim H.J., Yang A.Y., Kim S.W., Jeon E.J., Park J.H., Leem J, & Park K.K. (2019). Pharmacological Activation of Sirt1 Ameliorates Cisplatin-Induced Acute Kidney Injury by Suppressing Apoptosis, Oxidative Stress, and Inflammation in Mice. Antioxidants, 8(8), 322.
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Publication 2019
4-hydroxy-2-nonenal Antibodies Eosin Galectin 3 HAVCR1 protein, human Hematoxylin Injuries Kidney LCN2 protein, human Mice, House Microscopy, Confocal Microtomy Paraffin Paraffin Embedding paraform Periodic Acid Phosphates Stains Tissues

Most recents protocols related to «Galectin 3»

1
Efficient Antibody Generation via mRNA Immunization
Not available on PMC !

Example 4

An overview of the immunization strategies for lectin-binding proteins, such as galectin-3, is shown in Table 18.

BALB/c mice were immunized with 2 mg/kg mRNA, complexed with LNPs, or 20 μg recombinant protein as indicated in Table 18. Plasma anti-galectin-3 IgG titers were assayed 7 days after the final boost, which was delivered at day 55.

FIG. 3 shows that the use of galectin-3 mRNA as a final boosting agent resulted in a significantly higher target-specific IgG titer than when purified recombinant protein (a traditional immunogen) was used. This effect was observed regardless of whether the antigens were delivered subcutaneously or intravenously.

Hybridomas producing galectin-3-specific antibodies were generated, and high affinity monoclonal anti-galectin-3 antibodies were obtained from further screens.

TABLE 18
Priming ImmunizationBoostFinal Boost
(Day 0)(Day 7)(Day 55)
mRNA (I.V.)mRNA (I.V.)mRNA (I.V.)
mRNA (I.V.)mRNA (I.V.)Recombinant protein
(I.V.)
mRNA (S.C.)mRNA (S.C.)mRNA (S.C.)
mRNA (S.C.)mRNA (S.C.)Recombinant protein
(S.C.)
Summary of the Hit Rates Attainable by mRNA-Mediated Immunization

Table 19 provides a target protein-specific summary of the total number of hybridoma wells (generally about one third (⅓) of these wells contain hybridomas) screened and the number of confirmed target-specific antibodies obtained from those hybridomas wells following the use of lipid-encapsulated mRNA as an immunogen.

Table 20 provides a comparison of mRNA-LNP immunization methods with other conventional methods of immunization by number of hybridomas producing target-specific antibodies. In general, these data suggest that mRNA-LNP immunization is an effective method for inducing an immune response to a target protein antigen and for obtaining a higher number/rate of target protein-specific antibodies. In particular, these results confirm that mRNA-LNP immunization is surprisingly more effective than conventional immunization methods for obtaining antibodies specific for transmembrane proteins, e.g., multi-pass transmembrane proteins, such as GPCRs, which are difficult to raise antibodies against, and for poorly immunogenic proteins (e.g., proteins which produce low or no detectable target-specific IgGs in plasma of animals immunized with traditional antigen).

TABLE 19
Number of
Number ofhybridomas
hybridomaproducing
Proteinwellstarget-specific
targetType of proteinscreenedantibodies
RXFP1Multi-pass Transmembrane20240207
protein/GPCR
SLC52A2Multi-pass Transmembrane12880228
protein
ANGPTL8Soluble protein22816542
TSHRTransmembraneTBD130
protein/GPCR
APJTransmembrane22080230
protein/GPCR
GP130Single-pass Transmembrane23920614
protein

TABLE 20
Method of immunization and number of hybridomas producing
target-specific antibodies
Whole Virus-likeProtein/
ProteinType ofmRNA-cellsparticlesCDNApeptide
targetproteinLNP1onlyonlyonlyonly
RXFP1GPCR/20766NDNDND
multi-pass
SLC52A2multi-228NSTNSTNDNST
pass
TSHRGPCR/130NDND 42413
multi-pass
APJGPCR/230 94621 ND
multi-pass
1Immunization with mRNA-LNP alone or in combination with another antigen format (e.g., protein/peptide).
2Sanders et al. 2002 Thyroid stimulating monoclonal antibodies Thyroid 12(12): 1043-1050.
3Oda et al. 2000. Epitope analysis of the human thyrotropin (TSH) receptor using monoclonal antibodies. Thyroid 10(12): 1051-1059.
ND—Not determined; antigen format not tested
NST—No specific titers detected. Because no target-specific IgG titers were detectable in plasma, hybridoma generation was not initiated on these groups.

In general, successful generation of hybridomas producing antigen-specific antibodies have been achieved for at least 15 different targets utilizing mRNA-LNP immunization methods as exemplified herein. These results show that the mRNA immunization methods described herein are capable of eliciting an immune response against a wide range of antigens (e.g., transmembrane proteins, for example multi-pass transmembrane proteins, such as GPCRs) in host animals, and are effective methods for producing high affinity monoclonal antibodies, which can serve as parentals for generation of chimeric variants, humanized variants, and affinity matured variants.

US11878060B2. mRNA-mediated immunization methods (2024-01-23). NOVARTIS AG [CH]. Inventors: John Dominy [US], Robert Dunn [US], Scott Glaser [US], Mark Keating [US], Carla Klattenhoff [US], Igor Splawski [US].
Full text: Click here
Patent 2024
Animals anti-IgG Antibodies Antigens Binding Proteins Cells Chimera DNA, Complementary Epitopes Galectin 3 Histocompatibility Antigens Class II Homo sapiens Hybridomas Integral Membrane Proteins Lectin Lipids Mice, Inbred BALB C Monoclonal Antibodies Parent Peptides Plasma Proteins Protein Targeting, Cellular Recombinant Proteins Response, Immune RNA, Messenger Soluble Glycoprotein 130 Thyroid Gland Thyrotropin Thyrotropin Receptor Vaccination Viral Proteins
2
Quantifying Galectin-3-LRP1 Interactions
96-well plates were coated with recombinant human IgG1.Fc (A42561; Invitrogen) or human LRP-1 Cluster II Fc Chimera Protein covering ∼10% of the full-length Lpr1 protein sequence, including 3 N-glycosylation sites (#2368-L2-050; R&D Systems) at 0.5 μg in 100 μl PBS, incubated at 4°C overnight, and blocked with 50 mg/ml BSA for 90 min at 30°C. Serial concentrations ranging from 0.1 to 3.2 μg of recombinant human GALECTIN-3 (#774408; Biolegend), and test agents were added in a total volume of 50 μl and then incubated for 4 h at 30°C. Wells were washed, fixed with 2% PFA in PBS for 15 min at room temperature, washed, and incubated with rat anti-mouse monoclonal galectin-3 antibody (#125401; Biolegend; clone M3/38, epitopes mapped within the N-terminal region) for 30 min on ice. After washing, wells were incubated with AF488-conjugated donkey anti-rat secondary antibody (A-21208; Invitrogen Molecular Probes) for 30 min on ice. After washing, fluorescence was determined using a SpectraMax L (Molecular Devices) plate reader (excitation 485, emission 538) to quantify galectin-3–Lrp1 binding.
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
Amino Acid Sequence Antibodies, Anti-Idiotypic Chimera Clone Cells Epitopes Equus asinus Fluorescence Galectin 3 Homo sapiens IgG1 LGALS3 protein, human Medical Devices Mice, House Molecular Probes Monoclonal Antibodies NR4A2 protein, human Protein Glycosylation
3
Protein Extraction and Immunoblotting Methodology
Cell lysate preparation, SDS-PAGE, and Western blotting were carried out according to standard protocol. Proteins were harvested in cell lysis buffer supplemented with proteinase inhibitor cocktail (P8340; Sigma-Aldrich) and phosphatase inhibitor cocktail 2 (P5726; Sigma-Aldrich). Antigen detection was performed using antibodies directed against c-Src (rabbit anti-mouse/human antibody; #2109; Cell Signaling), Ctsk (mouse anti-mouse/human antibody; sc-48353; Santa Cruz), Rho (mouse anti-mouse/human antibody; #05-778; Millipore), galectin-3 (mouse anti-mouse/human antibody; ab2785; Abcam; epitopes mapped within the N-terminal region), Lrp1 (mouse anti-mouse antibody; MABN1796; Millipore), Mmp9 (rabbit anti-mouse antibody; ab38898; Abcam), Mmp14 (rabbit anti-mouse antibody; ab53712; Abcam), OXPHOS (rabbit anti-mouse antibody; ab110413; Abcam), vinculin (mouse anti-mouse antibody; V9131; Sigma-Aldrich), β3 integrin (rabbit anti-mouse antibody; #4702; Cell Signaling), or β-actin (rabbit anti-mouse antibody; #4970; Cell Signaling). Goat anti-rabbit IgG horseradish peroxidase (#65-6120; Thermofisher Scientific) or goat anti-mouse IgG horseradish peroxidase (#32430; Thermofisher Scientific) were used as secondary antibody. Bound primary antibodies (diluted to 1:1,000) were detected with horseradish peroxidase–conjugated species-specific secondary antibodies (Santa Cruz; diluted to 1:2,000) using the Super Signal Pico system (Thermo Fisher Scientific).
For immunoprecipitation analysis, cells were solubilized in IP Lysis Buffer (#87788; Thermo Fisher Scientific) supplemented with complete protease inhibitor cocktail (Roche). Immunoprecipitation was performed by incubation with a mouse monoclonal IgG (#5415; Cell Signaling) or anti–galectin-3 antibody (sc-32790; Santa Cruz) followed by the addition of Protein A/G Magnetic Beads (#88803; Thermo Fisher Scientific). Immune complexes were separated by electrophoresis followed by blotting with antibodies directed against Lrp1 (MABN1796; Millipore) and galectin-3 (ab2785; Abcam).
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
Actins anti-IgG Antibodies Antibodies, Anti-Idiotypic Antigens Buffers Cells Complex, Immune CTSK protein, human Electrophoresis Epitopes G-substrate Galectin 3 Goat GTP-Binding Proteins Homo sapiens Horseradish Peroxidase Immunoglobulins Immunoprecipitation Integrin beta3 MMP9 protein, human MMP14 protein, human Mus Protease Inhibitors protein phosphatase inhibitor-2 Proteins Rabbits SDS-PAGE Staphylococcal Protein A Vinculin
4
Osteoclast Dysfunction Pathways
Fig. S1 displays mitochondrial abundance and OXPHOS expression in Mmp9/Mmp14 DKO osteoclasts. Fig. S2 shows the identification and quantitative analysis of the metabolome in Mmp9/Mmp14 DKO osteoclasts. Fig. S3 depicts that active RhoA rescues defects in sealing zone formation and bone resorption in DKO osteoclasts. Fig. S4 shows that galectin-3 surface binding antagonist reverses functional defects in DKO osteoclasts. Fig. S5 depicts a galectin-3–Lrp1 axis regulates RhoA activation and sealing zone formation in osteoclasts. Table S1 is the list of the genotyping PCR primers. Table S2 lists the quantitative real-time PCR primers. Table S3 shows the list of galectin-3 interacting partners through mass spectrometry.
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
Bone Resorption Epistropheus Galectin 3 Mass Spectrometry Metabolome Mitochondria MMP9 protein, human MMP14 protein, human Oligonucleotide Primers Osteoclasts Real-Time Polymerase Chain Reaction RHOA protein, human
5
Calvarial Bone Resorption Assay
Calvariae from 5-d-old wild-type or DKO mice were isolated aseptically, cleaned, and cultured for 16 h at 37°C in 0.5 ml of BGJb medium (Life Technologies) containing 1 mg/ml BSA (fraction V; Sigma-Aldrich; Moxon et al., 2015 (link)). Half calvariae were transferred to fresh medium with 0.1 μM parathyroid hormone (H-4835.0005; Bachem) in the presence or absence of an anti–galectin-3 monoclonal antibody (sc-32790L; Santa Cruz) or an anti-Lrp1 monoclonal antibody (MA1-27198; Thermo Fisher Scientific), and cultured for an additional 5 d. Culture supernatant was collected for bone resorption marker CTX-I level detection using RatLaps CTX-I EIA kit (AC-06F1; Immunodiagnostic Systems). The half calvariae were either fixed for immunostaining with an anti-TRAP polyclonal antibody (sc-30833; Santa Cruz), an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38), or an anti-V-type proton pump-3 (Vpp3) polyclonal antibody (ab200839; Abcam) as describe above or snap-frozen for TRAP activity assay.
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 Biological Assay Bone Resorption Calvaria Clone Cells Freezing Galectin 3 Immunodiagnosis Immunoglobulins Monoclonal Antibodies Mus Parathyroid Hormone Physiotens Protons

Top products related to «Galectin 3»

1
Trizol reagent by Thermo Fisher Scientific
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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.
2
Galectin 3 by Abcam
Sourced in United States, United Kingdom, China
Galectin-3 is a protein that binds to beta-galactoside sugars and is involved in various biological processes. It is a member of the galectin family of proteins and is expressed in a variety of cell types. Galectin-3 plays a role in cell-cell and cell-matrix interactions, as well as in the regulation of cell growth and apoptosis.
3
Galectin 3 by R&D Systems
Sourced in United Kingdom, United States
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.
4
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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Anti-galectin-3 is a laboratory antibody product used for the detection and study of galectin-3, a carbohydrate-binding protein involved in various biological processes. This product is intended for research use only.

More about "Galectin 3"

Galectin-3, also known as Mac-2 antigen or L-29, is a member of the galectin family of beta-galactoside-binding lectins.
It plays a crucial role in various biological processes, including cell growth, differentiation, apoptosis, and immune regulation.
This multifunctional protein has been implicated in the pathogenesis of several diseases, such as cancer, fibrosis, and inflammation.
Galectin-3 is expressed in a variety of cell types, including epithelial cells, immune cells, and fibroblasts.
It can be found both intracellularly and extracellularly, and its functions are mediated through binding to specific carbohydrate moieties on cell surface glycoproteins and glycolipids.
Researchers can leverage PubCompare.ai, an AI-powered platform, to enhance their Galectin-3 research by locating protocols from literature, pre-prints, and patents.
By utilizing AI-driven comparisons, researchers can identify the best protocols and products for their studies, helping to optimize reproducibility and accuracy.
When studying Galectin-3, researchers may also incorporate other relevant tools and reagents, such as TRIzol reagent for RNA extraction, Lipofectamine 2000 for transfection, CL8942AP for Galectin-3 detection, FBS for cell culture, High-Capacity cDNA Reverse Transcription Kit for cDNA synthesis, and Bovine serum albumin (BSA) as a blocking agent.
Additionally, the use of Anti-galectin-3 antibodies can be valuable for immunological and biochemical analyses.
By leveraging these insights and resources, researchers can further expand their understanding of Galectin-3 and its role in various biological processes and disease states, ultimately contributing to advancements in the field.