Galectin-3/LGALS3 Protein, Human

Galectin-3/LGALS3 Protein is a type of galactoside-binding lectin that has a high binding affinity for carbohydrates with β-galactoside linkages. Galectin-3/LGALS3 Protein interacts with glycosylated proteins to mediate intercellular interactions and adhesion to the extracellular matrix. Galectin-3/LGALS3 Protein plays various roles, including regulating signaling pathways such as Wnt/β-catenin, affecting cell proliferation and survival, modulating immune functions, and influencing tumor progression. Galectin-3/LGALS3 Protein, Human is a recombinant galectin-3/LGALS3 protein expressed in E. coli^[1][2].

Galectin-3/LGALS3 Protein is widely distributed in most tissues and is extensively expressed in specific tissues, with extracellular, membrane-bound, cytoplasmic, and nuclear localization^[1].
The preferred ligand for Galectin-3/LGALS3 Protein is N-acetylglucosamine, which is also the only galectin that contains a conserved N domain and a single carbohydrate recognition domain (CRD). The N domain allows the formation of multimer complexes with proteins that do not bind to carbohydrate targets^[1].
Galectin-3/LGALS3 Protein has a variety of cell functions, including regulating environment-sensitive cell adhesion or splitting, modulating clathrin-independent endocytosis, controlling intracellular signaling through interactions with membrane-bound signal complexes, regulating Wnt/β-catenin signaling, affecting the activity of transcription factors like TTF-1 and STAT, influencing mRNA maturation by affecting spliceosome function, repairing DNA damage, inducing late G1 cell cycle arrest, promoting cell proliferation, and enhancing cell survival through anti-apoptotic effects via Bcl2^[1].
Galectin-3/LGALS3 Protein is involved in immune function. It enhances innate immunity by cleaning up cellular debris, promoting the production of respiratory burst enzymes, serving as a specific phagocytic signal for MerTK, and acting as a warning signal in the central nervous system; additionally, it can promote adaptive immunity by regulating T cell activation^[2].
Galectin-3/LGALS3 Protein is closely related to pathological processes such as tumors, cardiovascular diseases, and acute kidney injury^[3][4][5].

High expression of Galectin-3/LGALS3 Protein in MI D1 macrophages can promote neutrophil degranulation and regulate myocardial infarction^[3].
Overexpression of Galectin-3/LGALS3 Protein in non-small cell lung cancer may be associated with the occurrence and development of lung cancer^[4].
The lack of expression of Galectin-3/LGALS3 Protein in DCT cells of LGALS3 gene knockdown mice can promote AGE-mediated cell apoptosis^[5].
The lack of expression of Galectin-3/LGALS3 Protein in metastatic melanoma cells where the LGALS3 gene is silenced can inhibit the expression of the pro-tumor gene autotaxin (ENPP2) and the transcription factor NFAT1^[6].

The lack of expression of the Galectin-3/LGALS3 Protein in LGALS3 mutant (LGALS3 ^-/-) mice leads to a more diverse circadian rhythm pattern in their eating, drinking, and exercise behaviors^[1].
The expression level of Galectin-3/LGALS3 Protein is elevated in mice with acute kidney injury caused by rhabdomyolysis (RIAKI), thereby providing protection to the distal nephron from damage mediated by AGEs^[5].
Galectin-3/LGALS3 Protein is not expressed in melanoma mice with silenced LGALS3 gene, thereby promoting melanoma growth and metastasis by inhibiting the expression of NFAT1 and autotaxin^[6].

Measured by the ability of the immobilized protein to support the adhesion of MOLT-4 human acute lymphoblastic leukemia cells. The ED₅₀ for this effect is 2.109 μg/mL.

Human

E. coli

Tag Free

P17931 (A2-I250)

3958  [NCBI]

ADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI

Approximately 29 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 50 mM HEPES, 5% Sucrose, 5% Mannitol, 0.06% Tween80, pH 7.5 or PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Chaudoin TR, et al. Mice lacking galectin-3 (Lgals3) function have decreased home cage movement. BMC Neurosci. 2018 May 2;19(1):27.  [Content Brief]

  [2]. Demetriou M, et al. Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature. 2001 Feb 8;409(6821):733-9.  [Content Brief]

  [3]. Chalise U, et al. Macrophages secrete murinoglobulin-1 and galectin-3 to regulate neutrophil degranulation after myocardial infarction. Mol Omics. 2022 Mar 28;18(3):186-195.  [Content Brief]

  [4]. Yoshimura A, et al. Increased expression of the LGALS3 (galectin 3) gene in human non-small-cell lung cancer. Genes Chromosomes Cancer. 2003 Jun;37(2):159-64.  [Content Brief]

  [5]. Kulow VA, et al. Galectin-3 protects distal convoluted tubules in rhabdomyolysis-induced kidney injury. Pflugers Arch. 2024 Jul 23.  [Content Brief]

  [6]. Braeuer RR, et al. Galectin-3 contributes to melanoma growth and metastasis via regulation of NFAT1 and autotaxin. Cancer Res. 2012 Nov 15;72(22):5757-66.  [Content Brief]