Analytical Data
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Gene name
Galectin-2/LGALS2
- Application
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Alternative Names
Beta-galactoside-binding lectin L-14-II HL14 Lactose-binding lectin 2 S-Lac lectin 2
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Species
Human
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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
P05162
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Expression Region
1-132aa
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Molecular Weight
41.6 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
Galectin-2 (LGALS2) is a member of the galectin family, a group of proteins that bind to β-galactoside sugars and play significant roles in various biological processes, including cell adhesion, immune response, and apoptosis. Research on Galectin-2 has gained traction due to its involvement in several physiological and pathological conditions, such as cancer, inflammatory diseases, and cardiovascular disorders. Notably, Galectin-2 has been implicated in tumor progression and metastasis, making it a potential target for therapeutic interventions. The recombinant expression of LGALS2 allows for the detailed study of its structural and functional properties, enabling researchers to investigate its molecular mechanisms and interactions within cellular environments. By producing LGALS2 as a recombinant protein, scientists can explore its role in modulating immune responses, understand its pathway modulation in disease contexts, and assess its potential as a biomarker for diagnostics or therapeutic targets. Furthermore, recombinant LGALS2 can serve as a valuable tool in drug discovery and the development of galectin inhibitors, which could lead to novel strategies for treating diseases where Galectin-2 is a crucial player. Continued research into this recombinant protein is essential for elucidating its biological significance and potential clinical applications.
