• Purity

  >97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to agglutinate human red blood cells. Hadari, Y.R.     et al. (2000) J. Cell Sci.     113:2385. The ED    ₅₀ for this effect is typically ≤10 μg/mL.

• Source

  E. coli-derived Met1-Trp317

• Accession #

• N-terminal Sequence    
  Analysis

  Met1

• Predicted Molecular Mass

  36 kDa

• SDS-PAGE

  36 kDa, reducing conditions

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Galectin-8

The galectins constitute a large family of carbohydrate-binding proteins with specificity for N?acetyl?lactosamine?containing glycoproteins. At least 14 mammalian galectins, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified to date. The galectins have been classified into the prototype galectins (?1, ?2, ?5, ?7, ?10, ?11, ?13, ?14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins (Galectin-3) containing one CRD linked to a nonlectin domain, and the tandem?repeat Galectins (?4, ?6, ?8, ?9, ?12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified non-classical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell-surface glycoproteins (1-4).

Galectin-8, also known as prostate carcinoma tumor antigen 1 (PCTA1) in human, is a tandem repeat?type galectin. Prototype (single CRD) isoforms arising through alternate gene splicing have also been identified (5). Galectin-8 is highly expressed in lung carcinomas, certain forms of prostate carcinomas, as well as other tumor cells. It binds to a subset of cell surface integrins to modulate ECM?integrin interactions. As a soluble ligand, Galectin-8 can inhibit cell adhesion (6). Immobilized Galectin-8, however, has also been shown to promote cell adhesion (7). Human and mouse Galectin-8 share approximately 80% amino acid homology (4).

• References:

1. Rabinovich, A. et al. (2002) TRENDS in Immunol. 23:313.

2. Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.

3. Hughes, R.C. (2002) Biochimie 83:667.

4. R&D Systems’ Cytokine Bulletin, Summer, 2002.

5. Bidon, N. et al. (2001) Gene 274:253.

6. Hadari, Y. et al. (1995) J. Biol. Chem. 270:3447.

7. Levy, Y. et al. (2001) J. Biol. Chem. 276:31285.

• Entrez Gene IDs:

  3964 (Human)

• Alternate Names:

  GAL8; Gal-8; galectin 8; Galectin8; Galectin-8; galectin-8g; lectin, galactoside-binding, soluble, 8; LGALS8; PCTA1; PCTA-1Po66 carbohydrate-binding protein; Po66 carbohydrate binding protein; Po66-CBP; Prostate carcinoma tumor antigen 1