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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

Synonym(s):

ANTIGal-8, ANTILGALS8, ANTILectin, galectoside-binding, soluble 8, ANTIPCTA1, ANTIProstate carcinoma tumor antigen 1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

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.

O00214

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

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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.

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Human galectin-8 isoforms and cancer
Bidon WN and Le Pennec JP
Glycoconjugate Journal, 19(7-9), 557-563 (2002)
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
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
Nathalie Bidon-Wagner et al.
Glycoconjugate journal, 19(7-9), 557-563 (2004-02-06)
Galectins are animal lectins that can specifically bind beta-galactosides. Thirteen galectins have already been described. This review focuses on a specific member of this family: galectin-8. This galectin was discovered in prostate cancer cells eight years ago and has been
Yehiel Zick et al.
Glycoconjugate journal, 19(7-9), 517-526 (2004-02-06)
Galectin-8 belongs to the family of tandem-repeat type galectins. It consists as several isoforms, each made of two domains of approximately 140 amino-acids, both having a carbohydrate recognition domain (CRD). These domains are joined by a 'link peptide' of variable
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