Recombinant Mouse Galectin 8/Gal-8 protein is a Mouse Full Length protein, in the 1 to 316 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M L S L N N L Q N I I Y N P I I P Y V G T I T E Q L K P G S L I V I R G H V P K D S E R F Q V D F Q L G N S L K P R A D V A F H F N P R F K R S S C I V C N T L T Q E K W G W E E I T Y D M P F R K E K S F E I V F M V L K N K F Q V A V N G R H V L L Y A H R I S P E Q I D T V G I Y G K V N I H S I G F R F S S D L Q S M E T S A L G L T Q I N R E N I Q K P G K L Q L S L P F E A R L N A S M G P G R T V V I K G E V N T N A R S F N V D L V A G K T R D I A L H L N P R L N V K A F V R N S F L Q D A W G E E E R N I T C F P F S S G M Y F E M I I Y C D V R E F K V A I N G V H S L E Y K H R F K D L S S I D T L S V D G D I R L L D V R S W
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
Galectin-8, Gal-8, LGALS-8, Lgals8
Recombinant Mouse Galectin 8/Gal-8 protein is a Mouse Full Length protein, in the 1 to 316 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab134629 was purified using conventional chromatography techniques.
Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
Previously labelled as Galectin 8.
Galectin 8 also known as Gal-8 or GAL is a member of the galectin protein family which binds β-galactosides. The protein has another name anti-gal and possesses a molecular mass of approximately 36 kDa. It exhibits broad expression in various tissues including the immune system bones and gastrointestinal tract. Galectin-8 functions mechanically by binding to glycoproteins and glycolipids which facilitates cell adhesion and regulation processes.
Galectin-8 impacts numerous cellular functions through its involvement in immunomodulation and cell migration. Gal-8 promotes adhesion between cells and the extracellular matrix. It is not a part of a larger protein complex but interacts with multiple cell surface receptors guiding them toward or away from specific locations. Galectins including Galectin-8 influence immune cell responses by managing the apoptosis of T-cells and modifying cytokine production.
Galectin-8 engages in signaling pathways related to cellular adhesion and immune system modulation. It participates in the integrin-mediated cell adhesion pathway and contributes to the receptor signaling pathway associated with cytokines. Within these pathways Galectin-8 interacts with other proteins such as integrins and T-cell receptors influencing their activation internalization and cell surface retention.
Galectin-8 plays roles in cancer progression and inflammatory conditions. It is connected to cancer as it regulates angiogenesis cell invasion and metastasis. Galectin-8 interacts with fibronectin and vascular endothelial growth factor (VEGF) within the context of cancer. In inflammatory diseases Gal-8 influences immune cell migration and inflammation through its action on cytokine receptors contributing to conditions like rheumatoid arthritis.
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15% SDS-PAGE analysis of ab134629 (3μg)
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