Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
Greater than 95% as determined by SDS-PAGE.
LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.
LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
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.
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:
Recombinant Galectin-3 is widely used in research to study its role in various diseases and biological processes. Some key applications include: