Analytical Data
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Gene name
Lgals6
- Application
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Alternative Names
Lgals6; Galectin-6; Gal-6
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Species
Mouse
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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
O54891
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Expression Region
1-301aa
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Molecular Weight
61.1 kDa
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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
Research on LGALS6, a member of the galectin family, has garnered significant attention due to its potential implications in various biological processes and disease mechanisms. Galectins, a group of carbohydrate-binding proteins, play critical roles in cell-cell interactions, immune responses, and inflammation. LGALS6, specifically, is known to be involved in modulating cellular functions through its ability to bind to glycoproteins, influencing signal transduction pathways. Its expression has been linked to several pathological conditions, including cancer, autoimmune diseases, and infectious diseases, suggesting that it may serve as a valuable biomarker or therapeutic target. Recent studies have focused on the functional characterization of LGALS6, including its role in tumor progression and immune evasion. Additionally, recombinant LGALS6 proteins are being explored for their utility in both research and clinical applications, such as drug delivery systems and targeted therapies. Understanding the structure-function relationship of LGALS6, along with its interactions with other cellular components, could provide insights into its biological roles and pave the way for novel therapeutic strategies. Overall, LGALS6 represents a promising avenue for research that bridges basic science and clinical applications, highlighting the importance of further investigations into its mechanisms of action and potential for therapeutic intervention.
