Recombinant Human Galectin-3 Protein (LGALS3)

Beta LifeScience SKU/CAT #: BLC-05672P

Recombinant Human Galectin-3 Protein (LGALS3)

Beta LifeScience SKU/CAT #: BLC-05672P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description Recombinant Human Galectin-3 Protein (LGALS3) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin Less than 1.0 EU/μg as determined by LAL method.
Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to agglutinate human red blood cells is less than 10 μg/ml.
Uniprotkb P17931
Target Symbol LGALS3
Synonyms 35 kDa lectin; Carbohydrate binding protein 35; Carbohydrate-binding protein 35; CBP 35; CBP35; Gal-3; GAL3; Galactose-specific lectin 3; Galactoside-binding protein; GALBP; Galectin 3 internal gene,included; Galectin-3; Galectin3; GALIG; GBP; IgE binding protein; IgE-binding protein; L 31; L 34; L-31; L-34 galactoside-binding lectin; L31; Laminin-binding protein; Lectin L-29; Lectin, galactose binding, soluble 3; LEG3_HUMAN; LGALS2; LGALS3; MAC 2 antigen; Mac-2; Mac-2 antigen; MAC2; Macrophage galactose-specific lectin; MGC105387
Species Homo sapiens (Human)
Expression System E.Coli
Tag Tag-Free
Complete Sequence ADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI
Expression Range 2-250aa
Protein Length Full Length of Mature Protein
Mol. Weight 26.0 kDa
Research Area Neuroscience
Form Liquid or Lyophilized powder
Buffer Lyophilized from a 0.2 µm filtered solution in 1×PBS, 5% Trehalose, 0.02% Tween-20, 3mM β-ME, pH 7.4.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.

Target Details

Target Function Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes.
Subcellular Location Cytoplasm. Nucleus. Secreted.
Database References

HGNC: 6563

OMIM: 153619

KEGG: hsa:3958

STRING: 9606.ENSP00000254301

UniGene: PMID: 29248489

  • Interaction between galectin-3 and its potential inhibitor, bergenin, was studied using computational methods. PMID: 30276553
  • It has been reported that the Galectin-3/NuMA interaction is functionally important for the spindle pole organization; spindle pole cohesion requires glycosylation-mediated localization of NuMA. PMID: 28469279
  • The Mac-2-binding protein glycosylation isomer (M2BPGi), which is also known as Wisteria floribunda agglutinin-positive human Mac-2-binding protein, was recently established as a glycol-biomarker of liver fibrosis in patients with chronic hepatitis C with a unique fibrosis-related glycoalteration. PMID: 30128700
  • Higher plasma galectin-3 levels were associated with an elevated risk of developing incident chronic kidney disease, particularly among those with hypertension. PMID: 28865675
  • Pre-interventional plasma Galectin-3 levels are associated with left ventricular reverse remodeling and with clinical outcome after percutaneous mitral valve repair. PMID: 29678512
  • Galectin-3 is significantly associated with functional capacity, cardiac function and adverse cardiovascular events in adults with congenital heart defects. PMID: 28942393
  • Gene expression was analyzed for miR-1, miR-21, and galectin-3 in hypertensive patients with symptomatic heart failure and left ventricular hypertrophy. PMID: 29905364
  • Serum expression of miR-1 and miR-21, and the concentration of gal-3 in systolic heart failure patients with different degrees of left ventricular dilatation. PMID: 29905365
  • Serum galectin-3 is associated with coronary atherosclerosis and obstructive sleep apnoea syndrome (OSAS) severity in OSAS patients. PMID: 28150280
  • Study demonstrates that mesenchymal stromal cells (MSC)-derived LGALS3 may be critical for important biological pathways for MSC homeostasis and for regulating AML cell localization and survival in the leukemia microenvironmental niche. PMID: 29655803
  • Low expression of galectin-3 was detected in all patients with malignant gastrointestinal tumors irrespective of the presence of eosinophilia. PMID: 29926280
  • These findings highlight a new role for Galectin 3 as a non-classic RNA-binding protein that regulates MUC4 mRNA post-transcriptionally. PMID: 28262838
  • Galectin-3 is superior to sST2 in distinguishing HFpEF from controls and HFrEF. PMID: 30039808
  • erum Gal-3 levels were significantly higher in breast cancer (BC) patients and did not significantly differ according to clinical and tumoral characteristics of patients. Furthermore, there was no difference in Gal-3 levels between breast patients with and without metastatic disease. PMID: 30249872
  • Gal3 expression in regional lymph nodes might be associated with oral squamous cell carcinomas progression. The increased Gal3 expression in regional lymph nodes of larger tumors underlines the need of immunomodulatory treatment concepts in early-stage oral squamous cell carcinomas . Blocking of Gal3 might be a therapeutic option in oral cancer. PMID: 30115022
  • High Gal-3 serum levels predict fibrosis of the atrial appendage. PMID: 28079145
  • this study reviews the role of galectin-3 in Atrial Fibrillation mechanisms and its potential therapeutic implications. PMID: 29587379
  • Our findings provide evidence that allele C of rs4652 and allele T of rs11125 in the galectin-3 gene may be risk factors for cervical cancer. PMID: 28848207
  • High GAL-3 expression is associated with Salivary Gland Tumor. PMID: 29580041
  • Galectin-3 is greatly reduced in patients with cutaneous lupus lesions compared with healthy controls, which may contribute to the recruitment of inflammatory cells in the skin. PMID: 29058991
  • Progesterone receptor, EGFR, and galectin-3 are expressed differentially in uterine smooth muscle tumors. PMID: 29729689
  • Galectin-3 belongs to a class of inflammatory mediators that is associated with the degree of myocardial inflammation and fibrosis. It is related to the severity of myocardial ischemia and is negatively correlated with the cardiac ejection fraction. PMID: 29287900
  • Increased GAL-3 levels are an independent predictor of all-cause mortality in hemodialysis patients. PMID: 26787685
  • High GAL3 expression is associated with oral squamous cell carcinomas. PMID: 29284429
  • High expression level of Galectin-3 and low expression level of TRAIL were found to be positively correlated with the shorter median survival time and overall survival time. PMID: 28925481
  • Galectin-3 is overexpressed in patients with thyroid nodules, and can be used for diagnostic imaging and therapeutic targeting of cancer patients. (Review) PMID: 29393868
  • With emerging evidence to support the function and application of galectin3, the current review aims to summarize the latest literature regarding the biomarker characteristics and potential therapeutic application of galectin3 in associated diseases. PMID: 29207027
  • Our results indicate that concomitant stimulation and colocalization of galectin-3 with CD147 are associated with increased gelatinolytic activity in the actively ulcerating human cornea PMID: 29340650
  • Galectin-3 can be used as a biomarker for the prognosis evaluation of acute heart failure, and its combined analysis can increase the predictive value of NT-proBNP PMID: 29077153
  • Galectin has been identified as a proinflammatory protein and modulates immune responses either as damage-associated molecular patterns or as pattern recognition receptors. PMID: 28828226
  • Gal-3 was found to be significantly higher in the stroma of patients with H. pylori infection, mainly on Cag-A positive H. pylori, with chronic gastritis. PMID: 28939284
  • The present study demonstrates a relationship between galectin-3 levels and total body fat, abdominal fat, body fat distribution, cardiac size and geometry, and increase in total body fat over 2 years in young children. PMID: 29327139
  • Results suggest that galectin-3 could help to monitor the risk of short-term mortality in unselected patients with acute heart failure (AHF) attended in the emergency department (ED). PMID: 28406038
  • Report establishes the functional significance of Gal-3 as a broad-spectrum upstream effector in osteoarthritis (OA). A positive correlation between cartilage degeneration and Gal-3 positivity in chondrocytes and the ECM was found. PMID: 27982117
  • the secretion of galectin-3 as a novel mechanism for osteoblasts to control osteoclastogenesis and to maintain trabecular bone homeostasis independently of the RANKL/OPG-axis. PMID: 28822790
  • Gal-3 plasma concentration was significantly higher in pulmonary arterial hypertension patients. PMID: 28826890
  • Galectin-3 was associated with incident ischaemic stroke in younger but not older individuals. PMID: 28872212
  • As MUC1 and galectin-3 are both commonly overexpressed in most types of epithelial cancers, their interaction and impact on EGFR activation likely makes important contribution to EGFR-associated tumorigenesis and cancer progression. PMID: 28731466
  • serum Gal-3 is increased in Acute exacerbation of chronic obstructive pulmonary disease patients. PMID: 28947730
  • High serum levels of galectin-3 were found in patients with schizophrenia compared with that in controls. PMID: 28698921
  • N-linked glycoprotein maturation is not required for Gal-3 transport from the cytosol to the extracellular space, but is important for cell surface binding. Additionally, secreted Gal-3 is predominantly free and not packaged into extracellular vesicles. These data support a secretion pathway independent of N-linked glycoproteins and extracellular vesicles. PMID: 28775154
  • NRG1 and Gal-3 were significantly more elevated in cancer patients than in healthy controls. PMID: 28430337
  • discovery of site specific N-glycosylation changes of LGALS3BP in association of PDAC may provide useful clues to facilitate cancer detection or phenotype stratification PMID: 28627758
  • Our findings establish gal-3 as a molecular regulator of the JAG1/Notch-1 signaling pathway and have direct implications for the development of strategies aimed at controlling tumor angiogenesis. PMID: 28533486
  • findings reveal that differential levels of Gal-3 and Gal-8 expression and recruitment to Group A streptococcus (GAS) between epithelial cells and endothelial cells may contribute to the different outcomes of GAS elimination or survival and growth of GAS in these two types of cells. PMID: 28743815
  • The methylation frequency of the galectin-3 promoter was significantly higher while galectin-3 mRNA was lower in acute-on-chronic hepatitis B liver failure (ACHBLF) than in chronic hepatitis B and healthy controls. The results suggest that hypermethylation of the galectin-3 promoter might be an early biomarker for predicting disease severity and prognosis in patients with ACHBLF. PMID: 28185839
  • Serum Gal-3 and Nox4 levels were significantly elevated and correlated in 26 human pulmonary arterial hypertension patients when compared with 14 age- and sex-matched healthy controls. PMID: 28431936
  • These results demonstrate Tsc2-deficient mesenchymal progenitors cause aberrant morphogenic signals, and identify an expression signature including Lgals3 relevant for human disease of TSC1/TSC2 inactivation and mTORC1 hyperactivity. PMID: 28695825
  • Galectin-3 is a possible immunological target molecule of the pathogenic auto-antibodies PMID: 27339072
  • FAQs

    Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

    Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

    Recently viewed