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G5671

Sigma-Aldrich

Anti-Galectin-8 antibody, Mouse monoclonal

~1.0 mg/mL, clone VA-11.25, purified from hybridoma cell culture

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Synonym(s):
ANTIGal-8, ANTILGALS8, ANTILectin, galectoside-binding, soluble 8, ANTIPCTA1, ANTIProstate carcinoma tumor antigen 1
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

VA-11.25, monoclonal

form

buffered aqueous solution

mol wt

antigen ~34 kDa

species reactivity

mouse, rat, human

concentration

~1.0 mg/mL

technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 1-2 μg/mL using rat galectin 8 recombinant protein

isotype

IgM

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LGALS8(3964)
mouse ... Lgals8(56048)
rat ... Lgals8(116641)

Related Categories

General description

Galectins specifically bind to β-galactosides. 15 mammalian galectins have been identified so far. Galectin 8 contains two CRDs connected by a short linker peptide.
Monoclonal Anti-Galectin 8 (mouse IgM isotype) is derived from the hybridoma VA-11.25 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a recombinant rat galectin 8.Galectins belong to a family of carbohydrate-binding proteins. Within this family of proteins, galectin 8 is unique, as it exists in many forms encoded by the same gene.

Specificity

The antibody has low cross-reactivity with galectin 3 and galectin 9.

Immunogen

recombinant rat galectin 8.

application

Monoclonal Anti-galectin-8 antibody produced in mouse has been used for:
  • immunoblotting
  • immunocytochemistry
  • enzyme linked immunosorbent assay (ELISA)

Biochem/physiol Actions

Galectins belong to a family of carbohydrate-binding proteins. These proteins share similarities in the carbohydrate recognition domain (CRD) and in their specificity for N-Acetyllactosamine-enriched glycoconjugates. The binding of galectins to saccharides modulates cell proliferation, cell death and cell migration, which are involved in cancer initiation and progression. Galectin 8 is a secreted protein that requires both of its CRDs to be active to modulate cell adhesion. It forms a complex with integrins and triggers integrin-mediated signaling cascades. On the contrary, excessive amounts of this protein negatively regulate cell adhesion by interacting with integrins. These signals assist in identifying regions available for cell adhesion and migration. It may be involved in neoplastic transformation.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Human galectin-8 isoforms and cancer
Bidon WN and Le Pennec JP
Glycoconjugate Journal, 19(7-9), 557-563 (2002)
G A Rabinovich
Cell death and differentiation, 6(8), 711-721 (1999-09-01)
Galectins constitute a family of evolutionarily conserved animal lectins, which are defined by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and sequence similarities in the carbohydrate recognition domain. During the past decade, attempts to dissect the functional role for galectins in vivo
Laurent Ingrassia et al.
Current medicinal chemistry, 13(29), 3513-3527 (2006-12-16)
Galectins form a family of carbohydrate-binding proteins defined by their affinity for beta-galactosides containing glycoconjugates. The carbohydrate recognition domain (CRD) is responsible for the specificity of galectins for saccharides. This binding may result in modulated cell proliferation, cell death and
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
Hitomi Yamamoto et al.
Journal of biochemistry, 143(3), 311-324 (2007-11-21)
We previously showed that tandem-repeat type galectin-8, which has two covalently linked carbohydrate recognition domains (CRDs), induces neutrophil-adhesion through binding to integrin alphaM. Here, we analysed the function of galectin-8 in Jurkat T-cells. Galectin-8, as well as tandem-repeat galectin-9, and

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