Analytical Data
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Gene name
Galectin-8/LGALS8
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简介
Galectin-8 belongs to the family of animal lectins that bind to different glycoconjugates. Galectin-8 inhibits MTOR and AMPK signaling pathways to induce autophagy in response to lysosomal damage. Galectin-8 is highly expressed in a variety of tumors. Galectin-8/LGALS8 Protein, Rat (GST) is the recombinant rat-derived Galectin-8 protein, expressed by E. coli , with N-GST labeled tag.
- Application
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Alternative Names
Galectin-8; Gal-8; Po66 Carbohydrate-Binding Protein; Po66-CBP; Prostate Carcinoma Tumor Antigen 1; PCTA-1; LGALS8
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Species
Rat
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Source
E. coli
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Tag
N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6IN24
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Expression Region
M1-W316
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Protein Length
Full Length
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Molecular Weight
55kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Galectin-8 (LGALS8) is a member of the galectin family, a group of proteins known for their ability to bind beta-galactoside sugars, playing crucial roles in various biological processes, including cell adhesion, proliferation, and apoptosis. The expression of LGALS8 has been implicated in several physiological and pathological conditions, including cancer, inflammation, and autoimmune diseases. Its unique N-terminal and C-terminal domains allow it to interact with multiple partners, influencing cellular signaling pathways. Research has shown that LGALS8 can modulate immune responses and contribute to tumor progression by altering the tumor microenvironment and facilitating metastasis. Consequently, the study of LGALS8 is vital for understanding its functional roles in health and disease. The development of recombinant LGALS8 proteins has provided a valuable tool for investigating these mechanisms in vitro and in vivo, enabling researchers to dissect its biological functions, explore its therapeutic potentials, and evaluate its role as a biomarker for disease progression. As interest in galectins expands, LGALS8 stands out as a significant candidate for further exploration in targeted therapies and diagnostics, highlighting the need for continued research in this promising area of biomedical science.
