LGALS3 Mouse, Active
Description
Biochemical Properties of LGALS3 Mouse, Active
Formulation and Stability
Biological Activity
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Functional Assay: Agglutinates human red blood cells with an ED50 ≥25 µg/ml .
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Binding Partners: Interacts with TLR2, TLR6, integrins, and immune receptors to modulate inflammation and phagocytosis .
Role in Inflammation and Fibrosis
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Myeloid-Specific Depletion:
| Model | Outcome | Citation |
|---|---|---|
| Acute lung injury (LPS) | Reduced histology inflammation scores and interstitial neutrophils | |
| Chronic bleomycin | Decreased collagen deposition and fibrotic markers |
Immune Regulation
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Macrophage Polarization:
Neuroinflammation and Disease
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Microglial Activation:
Cell-Type-Specific Functions
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Neutrophils:
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Osteoblasts/Osteoclasts:
Molecular Interactions
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Ligands: Binds IgE, CSPG4, and DAMPs (damage-associated molecular patterns) .
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Post-Translational Regulation: MMP-12 cleaves Gal-3 into a 22-kDa fragment, modulating its proinflammatory effects .
Therapeutic Targeting
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Inhibitors: GB0139 (TD139), an inhaled Gal-3 inhibitor, reduced fibrosis in preclinical trials and is under Phase IIb evaluation for IPF .
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Biomarker Potential: Elevated serum Gal-3 predicts mild cognitive impairment (MCI) in type 2 diabetes and correlates with microglial activation in AD .
Preclinical Outcomes
Product Specs
Galectin-3 (LGALS3) is a member of the animal lectin family known for its binding affinity to beta-galactoside residues. This protein, synthesized within cells, is secreted through a process called ectocytosis. LGALS3 has been implicated in inhibiting apoptosis and potentially contributing to cancer development. Found in various epithelial tissues, it is also present in immune cells like dendritic cells, Kupffer cells, and macrophages. Elevated levels of LGALS3 are often observed during inflammation, cell proliferation, cell differentiation, and in cases of trans-activation by viral proteins.
This product consists of recombinant LGALS3 protein derived from mice and produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 287 amino acids (specifically, amino acids 1 to 264), resulting in a molecular mass of 29.8 kDa. The LGALS3 protein is fused to a 23 amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic methods.
The LGALS3 protein is supplied in a solution at a concentration of 0.5 mg/ml. The solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 1mM DTT, and 2mM EDTA.
For short-term storage (2-4 weeks), the product should be kept refrigerated at 4°C. For longer storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain product integrity, repeated freeze-thaw cycles should be avoided.
The purity of the LGALS3 protein is greater than 95% as determined by SDS-PAGE analysis.
The biological activity of this product is assessed based on its ability to cause the clumping (agglutination) of human red blood cells. The ED50 for this effect is determined to be greater than or equal to 25 µg/ml.
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
Q&A
Basic Research Questions
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What is the functional role of LGALS3 in murine neuroinflammatory models?
LGALS3 (Galectin-3) drives microglial activation and modulates neuroinflammatory responses in Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS), and tauopathy models. Its interaction with receptors like TLR4 and TREM2 promotes proinflammatory phenotypes, while its absence exacerbates pathology in ALS but ameliorates it in AD . -
Which transgenic mouse models are best suited for studying LGALS3 in immune regulation?
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APP/PS1 and 5xFAD mice: For AD studies, these models show LGALS3 upregulation in microglia, correlating with amyloid-β plaque burden .
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SOD1 G93A mice: For ALS, LGALS3 deletion accelerates disease progression, highlighting its context-dependent role .
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DSS-induced colitis models: LGALS3 modulates innate lymphoid cells (ILC3s) and neutrophil recruitment .
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Advanced Research Questions
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How to reconcile contradictory findings on LGALS3’s neuroprotective vs. neurotoxic roles?
LGALS3 exhibits dual roles depending on disease context:-
Neurotoxic in AD: Promotes tau hyperphosphorylation and microglial inflammatory responses .
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Neuroprotective in ALS: Stabilizes motor neuron integrity via lysosomal repair mechanisms .
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Experimental Design: Conduct comparative studies using Lgals3 / − mice across multiple models (e.g., AD vs. ALS). Use single-cell RNA sequencing to map microglial subtypes and LGALS3-associated pathways .
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What are the limitations of current LGALS3-targeted interventions in preclinical studies?
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Off-target effects: LGALS3 interacts with multiple receptors (TLR4, TREM2, MerTK), complicating therapeutic targeting .
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Model-specific variability: Myeloid-specific deletion (LysM-cre) reduces LGALS3 in neutrophils and macrophages but not fully in epithelial cells, affecting lung injury outcomes .
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Recommendation: Use tissue-specific promoters (e.g., Cx3cr1-cre for microglia) and validate with spatial transcriptomics .
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Data Contradictions and Resolution Strategies
Methodological Recommendations
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How to design a longitudinal study assessing LGALS3 in chronic vs. acute inflammation?
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What biomarkers complement LGALS3 in profiling microglial activation?
Integration with Multi-Omics Data
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How to contextualize LGALS3 within microglial metabolic modules?
Product Science Overview
Galectin-3 is a member of the galectin family, which are beta-galactoside-binding proteins involved in various cellular functions. This protein is encoded by the LGALS3 gene and is known for its role in cell-cell adhesion, cell-matrix interactions, and intracellular signaling. Galectin-3 is found in various tissues and cell types, including immune cells, epithelial cells, and fibroblasts.
Galectin-3 is a chimeric protein composed of a carbohydrate recognition domain (CRD) and a non-lectin domain. The CRD allows Galectin-3 to bind to beta-galactoside residues on glycoproteins and glycolipids. This binding capability is crucial for its role in cellular processes such as apoptosis, immune response, and inflammation.
In its recombinant form, Galectin-3 is often produced in bacterial systems like Escherichia coli (E. coli) or mammalian cell lines such as HEK293. The recombinant protein retains its bioactivity and is used in various research applications, including studies on cancer, fibrosis, and immune regulation .
Galectin-3 has several biological activities:
- Apoptosis Inhibition: Galectin-3 can inhibit apoptosis, thereby promoting cell survival. This function is particularly relevant in cancer cells, where Galectin-3 expression is often upregulated.
- Immune Regulation: Galectin-3 modulates immune responses by affecting the function of various immune cells, including macrophages, T cells, and dendritic cells.
- Cell Adhesion and Migration: By binding to glycoproteins on the cell surface, Galectin-3 facilitates cell-cell and cell-matrix interactions, influencing cell adhesion and migration.
- Fibrosis: Galectin-3 is implicated in the development of fibrosis in various organs, including the liver, lungs, and heart. It promotes the activation of fibroblasts and the deposition of extracellular matrix components.
Recombinant Galectin-3 is widely used in research to study its role in various diseases and biological processes. Some key applications include:
- Cancer Research: Galectin-3 is used as a biomarker for cancer diagnosis and prognosis. It is also studied for its role in tumor progression, metastasis, and resistance to therapy .
- Fibrosis Studies: Researchers use Galectin-3 to investigate its role in fibrotic diseases and to develop potential therapeutic strategies to inhibit its activity.
- Immune Response: Galectin-3 is studied for its effects on immune cell function and its potential as a target for immunotherapy.
