Recombinant Human Galectin-8 Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human Galectin-8 Protein Summary

Details of Functionality
Measured by its ability to agglutinate human red blood cells. Hadari, Y.R. et al. (2000) J. Cell Sci. 113:2385. The ED50 for this effect is ≤10 μg/mL.
Source
E. coli-derived human Galectin-8 protein
Met1-Trp317
Accession #
N-terminal Sequence
Met1
Protein/Peptide Type
Recombinant Proteins
Gene
LGALS8
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
36 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
36 kDa, reducing conditions
Publications
Read Publications using
1305-GA in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, TCEP, PEG 8000 and Trehalose with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Galectin-8 Protein

  • 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

Background

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).

  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.

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1305-GA
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Applications: Bioactivity

Publications for Galectin-8 (1305-GA)(3)

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Bioinformatics

Gene Symbol LGALS8
Uniprot