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| 规格: | 100μg | 产品价格: | ¥2600.0 |
|---|---|---|---|
| 规格: | 500μg | 产品价格: | ¥10400.0 |
Galectin-3 (Gal-3) is a member of the galectin family of carbohydrate binding proteins which have affinity for beta-galactoside. Gal-3 is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. Gal-3 can self-associate through the N-terminal domain allowing it to bind to multivalent saccharide ligands. Gal-3 is expressed in the nucleus, cytoplasm, mitochondrion, cell surface and extracellular space, and plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion and T-cell regulation and exhibits antimicrobial activity against bacteria and fungi. Alternate splicing results in multiple transcript variants, Gal-3 plays an important role in the pathogenesis of neuroinflammatory and neurodegenerative disorders, such as multiple sclerosis, Alzheimer's disease, Parkinson's disease, and Huntington's disease. On the other hand, there is also evidence of the protective role of Gal-3 due to its anti-apoptotic effect in target cells.
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文献和实验Galectin-3 Binding and Metastasis
Galectin-3 is a member of a family of carbohydrate-binding proteins. It is present in the nucleus, the �cytoplasm, and also the extracellular matrix (ECM) of many normal and neoplastic cell types. Reports show an upregulation of this protein
Purification of Human Complement Protein C5
Complement C5 is cleaved by proteolysis in the terminal phase of complement activation generating the pro-inflammatory C5a and membrane attack complex nucleator C5b. Whereas purification of its paralogues C3 and C4 from plasma is relatively
Analysis of Protein Phosphorylation in Human Neutrophils
, serines and threonines. Upon covalent binding of phosphates to these amino acids, the charge and conformation of the corresponding proteins are modified, generally leading to changes in protein functions such as protein-protein interactions and enzymatic
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