LGALS2 Mouse, Active
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Greater than 95% as determined by SDS-PAGE.
Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.
LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Galectin-2, also known as LGALS2, belongs to the galectin family. These proteins are defined by their ability to bind carbohydrates (lectins) and play roles in cell-to-cell adhesion, cell-to-extracellular matrix interactions, pre-mRNA splicing, apoptosis, and tumor progression. Galectin-2 specifically has been shown to induce apoptosis in activated T cells, bind to lymphotoxin-a, and may be implicated in myocardial infarction. Human and mouse LGALS2 share approximately 65% amino acid sequence similarity.
Recombinant Mouse LGALS2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein contains 153 amino acids (including a 23 amino acid His-tag at the N-terminus, spanning residues 1-130 of the LGALS2 sequence) and has a molecular weight of 17.3 kDa. The protein is purified using proprietary chromatographic techniques.
LGALS2 protein is supplied at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is suggested for extended storage. Avoid repeated freeze-thaw cycles.
Purity is determined to be greater than 95% by SDS-PAGE analysis.
The biological activity of LGALS2 is assessed by its ability to agglutinate human red blood cells. The ED50, defined as the concentration required to achieve 50% agglutination, is greater than or equal to 20 µg/ml.
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
Product Science Overview
Galectin-2 is a member of the galectin family, which consists of carbohydrate-binding proteins known for their role in various cellular processes, including cell-cell adhesion, cell-matrix interactions, and intracellular signaling. Galectin-2, specifically, is a homodimeric protein with a molecular weight of approximately 14 kDa . It belongs to the S-type lectin family and contains a single carbohydrate-recognition domain (CRD) .
Galectin-2 is involved in modulating immune responses and has been shown to induce a proinflammatory phenotype in monocytes and macrophages . This protein plays a significant role in the regulation of inflammatory responses and has been associated with decreased collateral arteriogenesis in patients with obstructive coronary artery disease . The interaction of galectin-2 with CD14/TLR4 on monocytes leads to the induction of proinflammatory cytokines and inhibition of pro-arteriogenic factors .
Recombinant mouse galectin-2 is typically produced using human embryonic kidney (HEK293) cells . The gene encoding mouse galectin-2 is cloned into an expression vector, which is then transfected into HEK293 cells. The cells are cultured, and the recombinant protein is harvested from the culture medium. The protein is then purified using affinity chromatography techniques to ensure high purity and activity .
For large-scale production, recombinant mouse galectin-2 can be produced using bioreactor systems. The HEK293 cells expressing galectin-2 are grown in bioreactors under controlled conditions to maximize yield. The culture medium is continuously monitored and adjusted to maintain optimal growth conditions. After sufficient protein expression, the culture medium is collected, and the recombinant protein is purified using a series of chromatographic steps, including affinity chromatography and size-exclusion chromatography .
Galectin-2 binds to specific carbohydrate structures on the surface of cells, mediating various biological effects. The binding affinity of galectin-2 to its ligands is influenced by the presence of specific glycan structures. For instance, galectin-2 has been shown to interact with MUC5AC, a major gastric mucin glycoprotein, through affinity chromatography and subsequent LC-MS/MS analysis . This interaction highlights the specificity of galectin-2 for certain carbohydrate ligands and its potential role in modulating cellular functions through glycan recognition.
