Analytical Data
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Gene name
LGALSL
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简介
The LGALSL protein was identified as a member of the galectin family, exhibits no affinity for lactose, and may not be involved in carbohydrate binding. This unique feature distinguishes LGALSL from typical galectins, which are known for their carbohydrate recognition domain and interaction with specific sugar moieties. LGALSL Protein, Human (His) is the recombinant human-derived LGALSL protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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Alternative Names
Galectin-Related Protein; Lectin Galactoside-Binding-Like Protein; LGALSL; GRP; HSPC159
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q3ZCW2
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Expression Region
A2-G172
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Protein Length
Full Length of Mature Protein
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Molecular Weight
18.0 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
The LGALSL recombinant protein is derived from LGALS family of proteins, specifically galectin-5, which is known for its role in cell adhesion, immune response modulation, and apoptosis. Research into LGALSL has gained traction due to its potential implications in various biological processes and diseases, including cancer progression, inflammatory responses, and infection. Galectins, including LGALS, can influence tumor growth and metastasis by modulating cell signaling pathways and immune cell interactions. The recombinant production of LGALSL allows for detailed studies into its structural and functional properties, enabling researchers to investigate its binding affinities, carbohydrate recognition capabilities, and potential therapeutic applications. The study of LGALSL also provides insights into its possible roles in the development and progression of autoimmune diseases, further emphasizing its relevance in biomedical research. Understanding LGALSL at a molecular level may lead to the identification of novel biomarkers for disease diagnosis, progression, and treatment strategies. The increasing interest in galectins as therapeutic targets underlines the importance of characterizing LGALSL and exploring its biological functions in health and disease.
