Recombinant Human LGALS8 Protein

Name: Recombinant Human LGALS8 Protein
Brand: Beta LifeScience
SKU: BL-2023NP
Availability: InStock

BL-2023NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Galectin-8 is produced by our E.coli expression system and the target gene encoding Met1-Trp317 is expressed.
Accession	O00214
Synonym	Galectin-8; Gal-8; Po66 Carbohydrate-Binding Protein; Po66-CBP; Prostate Carcinoma Tumor Antigen 1; PCTA-1; LGALS8
Gene Background	The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. 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(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat 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 nonclassical 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.
Molecular Mass	35.8 KDa
Apmol Mass	32 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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

analysis of crystallographic structures of the galectin-8 N-terminal domain (galectin-8N) in complex with LNT and LNnT PMID: 28000747
Gal-8 served as a new positive prognostic factor for the OS and DFS of ovarian cancer patients. PMID: 29361803
the natural and conserved expression of Gal-8 in tumour cells is responsible for the metastatic evolution of prostate cancer. PMID: 28591719
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
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
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
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
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
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
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
The fundamental roles of galectin-8 in human anaplastic large cell lymphoma PMID: 25573487
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
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
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
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
analysis of how human Galectin-8C domain interacts with its glycan ligands PMID: 23555773
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
Association of galectin-8 (F19Y) occurrence with autoimmune diseases in a Caucasian population. PMID: 22683700
Galectin-8 promotes cytoskeletal rearrangement in trabecular meshwork cells through activation of Rho signaling. PMID: 22973445
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
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
a novel role for the tandem repeat Gal8 in promoting FV endocytosis. PMID: 22267735
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
Gal-8 was expressed by villous and extravillous cytotrophoblast. PMID: 21862124
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
Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. PMID: 21288902
Studies indicated that Gal-8 was expressed both in the cytoplasm and nucleus in ECs of normal and tumor vessels. PMID: 20876211
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
Galectin-8 up-regulation is associated with hypopharyngeal and laryngeal tumor progression. PMID: 20044599
The binding ability of galectin-8 to membrane-associated GM3 was confirmed using CHO cells, which predominantly express GM3 PMID: 12851289
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
REVIEW: isoforms and role in neoplastic transformation/cancer PMID: 14758080
galectin-8 is a modulator of cellular growth through up-regulation of p21 PMID: 15753078
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
The affinity of Gal-8 and its carbohydrate recognition domains for ligands in solution and at the cell surface is explored. PMID: 17339281
galectin-8 sorting is based on carbohydrate fine specificity PMID: 17580315
The function of galectin-8 in Jurkat T-cells, is analysed. PMID: 18024965
allows Gal-8 to signal phosphatidylserine exposure in leukocytes entirely through C-terminal domain recognition of polyLacNAc glycans PMID: 18456665
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
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
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
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
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.

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