Recombinant Human Galectin 8 Protein (GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-2187

Recombinant Human Galectin 8 Protein (GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-2187
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Product Overview

Host Species Human
Accession AAF19370.1
Synonym Gal-8, PCTA-1, PCTA1, Po66-CBP
Description A DNA sequence encoding human LGALS8 (AAF19370.1) (Met 1-Trp 317) was fused with the GST tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Trp 317
Molecular Weight The recombinant human LGALS8/GST chimera consists of 550 a.a. and predicts a molecular mass of 62.7 kDa. The apparent molecular mass of rh LGALS8/GST is approximately 60 kDa in SDS-PAGE under reducing conditions.
Purity >76% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is typically 0.2-1 ug/ml.
Formulation Lyophilized from sterile 50mM Tris, 0.1 M NaCl, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
Subcellular Location Cytoplasmic vesicle. Cytoplasm, cytosol.
Database References

HGNC: 6569

OMIM: 606099

KEGG: hsa:3964

UniGene: Hs.4082

Tissue Specificity Ubiquitous. Selective expression by prostate carcinomas versus normal prostate and benign prostatic hypertrophy.

Gene Functions References

  1. analysis of crystallographic structures of the galectin-8 N-terminal domain (galectin-8N) in complex with LNT and LNnT PMID: 28000747
  2. Gal-8 served as a new positive prognostic factor for the OS and DFS of ovarian cancer patients. PMID: 29361803
  3. the natural and conserved expression of Gal-8 in tumour cells is responsible for the metastatic evolution of prostate cancer. PMID: 28591719
  4. Both Gal-8 isoforms led to enhanced adhesion of myeloma cells to vascular endothelium under dynamic shear stress conditions, Gal-8L (by more than 40-fold) even stronger than Gal-8S. PMID: 27287437
  5. Our data indicate that Gal-8 interacts with ALCAM at the surface of breast cancer cells through glycosylation-dependent mechanisms. A novel heterophilic interaction between ALCAM and Gal-8 is demonstrated here, suggesting its physiologic relevance in the biology of breast cancer cells PMID: 27130882
  6. we detected Gal-8 in human cerebrospinal fluid, suggesting a role in the CNS immune-surveillance circuit. In addition, we show that MS patients generate function-blocking anti-Gal-8 antibodies with pathogenic potential. Furthermore, circulating anti-Gal-8 antibodies associate with relapsing-remitting MS, and not with progressive MS phenotypes, predicting clinical disability at diagnosis within the first year of follow-up PMID: 28650992
  7. Data suggest that galectin-8 is a potential independent favorable prognostic biomarker for survival and recurrence of patients with gastric cancer after surgery. PMID: 27444274
  8. this study uncovers a unique molecular mechanism of lymphangiogenesis in which galectin-8-dependent crosstalk among VEGF-C, podoplanin and integrin pathways plays a key role. PMID: 27066737
  9. Platelet-derived factor V/Va is generated following endocytosis of the plasma-derived molecule by the platelet precursor cells, megakaryocytes, via a two receptor system consisting of LRP-1 and an unidentified specific "binding site". PMID: 25800007
  10. Gal-8 expression is a potential independent unfavorable prognostic indicator for postoperative recurrence of patients with localized pT1 clear cell renal cell carcinoma PMID: 25499921
  11. The fundamental roles of galectin-8 in human anaplastic large cell lymphoma PMID: 25573487
  12. The implications of gal-8 in tumor angiogenesis remain to be further explored, but it is exciting to speculate that modulating gal-8-glycan interactions could be used to block lymphatic-vascular connections vital for metastasis PMID: 24939370
  13. We integrate here the available information on Gal-8 expression in different tumor types and attempt to elucidate associations of its expression and localization with tumor progression[review] PMID: 24696431
  14. these results not only confirm the pro-inflammatory role we have already proposed for Gal-8 in other cellular systems but also suggest that this lectin is orchestrating the interaction between leukocytes, platelets and endothelial cells PMID: 24957054
  15. Focusing on the F19Y change in galectin-8, we study of consequences of a single-site substitution in the carbohydrate recognition domain of this family of cellular effectors. PMID: 24418318
  16. analysis of how human Galectin-8C domain interacts with its glycan ligands PMID: 23555773
  17. Data indicate that the binding site in galectin-8 is essential for the recruitment of the autophagy receptor NDP52 to cytosol-exposed Salmonella Typhimurium. PMID: 23386746
  18. Association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population. PMID: 22683700
  19. Galectin-8 promotes cytoskeletal rearrangement in trabecular meshwork cells through activation of Rho signaling. PMID: 22973445
  20. Results indicate a difference in specificity between N-terminal and C-terminal carbohydrate recognition domains (N-CRD and C-CRD) of galectin-8. PMID: 22913484
  21. This is the first study that relates a galectin, an endogenous lectin family, to IgA nephritis and thus should stimulate new avenues of research into the pathophysiology of the disease. PMID: 22173878
  22. a novel role for the tandem repeat Gal8 in promoting FV endocytosis. PMID: 22267735
  23. results illustrate how cells deploy the danger receptor galectin 8 to combat infection by monitoring endosomal and lysosomal integrity on the basis of the specific lack of complex carbohydrates in the cytosol PMID: 22246324
  24. Gal-8 was expressed by villous and extravillous cytotrophoblast. PMID: 21862124
  25. galectin-8 loss might be an early step in the development of malignant lesions of the bladder and is a significant independent predictor of recurrence PMID: 21757871
  26. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. PMID: 21288902
  27. Studies indicated that Gal-8 was expressed both in the cytoplasm and nucleus in ECs of normal and tumor vessels. PMID: 20876211
  28. Platelets not only contain Gal-8, but also expose Gal-8 after thrombin activation. Findings reveal Gal-8 isoforms as a potent platelet activator; immobilized Gal-8 promotes platelet adhesion/spreading. PMID: 20858220
  29. Galectin-8 up-regulation is associated with hypopharyngeal and laryngeal tumor progression. PMID: 20044599
  30. The binding ability of galectin-8 to membrane-associated GM3 was confirmed using CHO cells, which predominantly express GM3 PMID: 12851289
  31. Human galectin-8 induced firm and reversible adhesion of peripheral blood neutrophils but not eosinophils to a plastic surface in a lactose-sensitive manner; galectin-8 is a novel factor that modulates the neutrophil function. PMID: 12881409
  32. REVIEW: isoforms and role in neoplastic transformation/cancer PMID: 14758080
  33. galectin-8 is a modulator of cellular growth through up-regulation of p21 PMID: 15753078
  34. Gal-8 constitutes a novel extracellular stimulus for T cells, able to bind specific beta1 integrins and to trigger signaling pathways conducive to cell spreading. PMID: 16368432
  35. The affinity of Gal-8 and its carbohydrate recognition domains for ligands in solution and at the cell surface is explored. PMID: 17339281
  36. galectin-8 sorting is based on carbohydrate fine specificity PMID: 17580315
  37. The function of galectin-8 in Jurkat T-cells, is analysed. PMID: 18024965
  38. allows Gal-8 to signal phosphatidylserine exposure in leukocytes entirely through C-terminal domain recognition of polyLacNAc glycans PMID: 18456665
  39. Gal8 modulates trabecular meshwork cell adhesion and spreading, at least in part, by interacting with alpha2-3-sialylated glycans on beta(1) integrins. PMID: 18849583
  40. Galectin-8 was expressed in the majority of papillary carcinomas. Positive but weaker staining was found in some of follicular thyroid carcinomas and adenomas. Galectin-8 found in hyperplastic areas adjacent to tumor was weakly positive in 9 of 31 cases. PMID: 19009371
  41. These data suggest a role for galectin-8 and podoplanin in supporting the connection of the lymphatic endothelium to the surrounding extracellular matrix, most likely in cooperation with other glycoproteins on the surface of lymphatic endothelial cells. PMID: 19268462
  42. The glycan-binding proteins of the galectin family can modulate the immune system. Anti-galectin autoantibodies thus could have functional and/or pathogenic implications in inflammatory processes and autoimmunity. PMID: 19395456
  43. crystal of a protease-resistant mutant form of human galectin-8 was obtained using the hanging-drop method and was found to belong to the tetragonal space group P4(3)2(1)2 PMID: 19407390


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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