G3670
Galectin-8 from rat
recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
Gal-8, Po66 carbohydrate-binding protein, Prostate carcinoma tumor antigen 1
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About This Item
MDL number:
UNSPSC Code:
12352202
biological source
rat
recombinant
expressed in E. coli
Assay
≥90% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
protein 34 kDa
packaging
pkg of 100 μg
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
rat ... Lgals8(116641)
General description
Galectin-8 is one of the β-galactoside-binding lectins called galectins, which reside in the cytosol before being released in a signal sequence-independent pathway.
Biochem/physiol Actions
Galectin-8 functions as a danger receptor and thus, prevents the proliferation of Salmonella. It detects host glycans found on the surface of damaged Salmonella-containing vacuoles. It also maintains the endo-lysosomal integrity. This protein prevents the adhesion of human carcinoma cells to integrin-ligand coated plates. This results in induction of apoptosis.
Galectin-8 is a family member of animal lectins which selectively binds β-galactoside residues. It is a widely expressed 34 kDa protein, which is secreted by many cell types. Galectin-8 is made of two homologous regions, each having a single carbohydrate recognition domain (CRD), linked by a short peptide. Galectin-8 acts as a physiological modulator of cell adhesion and cellular growth, and may be involved in neoplastic transformation.
Physical form
Solution containing 20 mM Tris, pH 7.4, 1 mM DTT, 1 mM EDTA, and 30% glycerol.
Analysis Note
The biological activity is measured by its ability to agglutinate human red cells.
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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Osamu Suzuki et al.
International journal of oncology, 46(3), 973-980 (2015-01-13)
The interaction between cell surface glycans and extracellular matrix (ECM) including galectins is known to be closely associated with tumor cell adhesion, invasion and metastasis. We analyzed the roles of cell surface sialylation or glycosylation in galectin or ECM‑mediated cell
Y Levy et al.
The Journal of biological chemistry, 276(33), 31285-31295 (2001-05-24)
The interaction of cells with the extracellular matrix regulates cell adhesion and motility. Here we demonstrate that different cell types adhere and spread when cultured in serum-free medium on immobilized galectin-8, a mammalian beta-galactoside-binding protein. At maximal doses, galectin-8 is
Teresa L M Thurston et al.
Nature, 482(7385), 414-418 (2012-01-17)
Autophagy defends the mammalian cytosol against bacterial infection. Efficient pathogen engulfment is mediated by cargo-selecting autophagy adaptors that rely on unidentified pattern-recognition or danger receptors to label invading pathogens as autophagy cargo, typically by polyubiquitin coating. Here we show in
I Camby et al.
Brain pathology (Zurich, Switzerland), 11(1), 12-26 (2001-01-06)
Galectins, a family of mammalian lectins with specificity to beta-galactosides, are involved in growth-regulatory mechanisms and cell adhesion. A relationship is assumed to exist between the levels of expression of galectins and the level of malignancy in human gliomas. A
Y R Hadari et al.
Journal of cell science, 113 ( Pt 13), 2385-2397 (2000-06-15)
The interaction of cells with the extracellular matrix regulates cell adhesion, motility, growth, survival and differentiation through integrin-mediated signal transduction. Here we demonstrate that galectin-8, a secreted mammalian (beta)-galactoside binding protein, inhibits adhesion of human carcinoma (1299) cells to plates
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