Analytical Data
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Gene name
Galectin
- Application
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Species
Angiostrongylus cantonensis
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Source
E. coli
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Tag
N- His-NusA
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
G1EUS2
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Expression Region
1-278aa
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Molecular Weight
92.5 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
Related Products
Protein Description
Galectins are a family of β-galactoside-binding proteins that play critical roles in various biological processes, including cell adhesion, proliferation, differentiation, and apoptosis. Their involvement in immune regulation and inflammatory responses has made them a focal point of research, particularly in the context of cancer, autoimmune diseases, and infection. Galectin-1, for instance, is known to modulate T-cell activity, while Galectin-3 has been implicated in tumor progression and metastasis. Consequently, the study of recombinant galectin proteins has gained momentum, as they serve as valuable tools for elucidating the molecular mechanisms underlying these diverse functions. Researchers are utilizing recombinant techniques to produce galectin proteins in vitro, enabling detailed structural and functional analyses. This approach not only aids in understanding galectin-ligand interactions but also facilitates the development of potential therapeutic applications, such as targeted cancer therapies and immunomodulators. Furthermore, the ability to generate large quantities of pure galectin proteins paves the way for high-throughput screening methods to identify galectin inhibitors or agonists, which could lead to novel treatment strategies. The ongoing exploration of galectin recombinants holds promise for advancing both basic and translational research in the fields of immunology and oncology, highlighting their significance as crucial players in health and disease.
