Analytical Data
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Gene name
LGALS8
- Application
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Alternative Names
LGALS8;Galectin-8
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00214
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Expression Region
1-317aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMMLSLNNLQNIIYNPVIPFVGTIPDQLDPG TLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNT LINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRI GPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGT PQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHL NPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKV AVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW
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Molecular Weight
38 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
LGALS8, also known as Galectin-8, is a member of the galectin family of carbohydrate-binding proteins, which play critical roles in various biological processes, including cell adhesion, proliferation, and apoptosis. The interest in LGALS8 arises from its involvement in diverse pathological conditions, including cancer, inflammation, and autoimmune diseases. Studies have shown that LGALS8 can modulate immune responses, influencing the behavior of immune cells and tumor microenvironments. Its dual-ligand binding ability enables LGALS8 to interact with different cellular receptors, promoting either pro-inflammatory or anti-inflammatory signals depending on the context. Understanding its structural properties and functional mechanisms is crucial for developing therapeutic strategies targeting LGALS8-related pathways. Recent advances in recombinant protein technology have made it possible to produce LGALS8 in a laboratory setting, allowing for detailed studies of its properties, interactions, and potential applications in biomedical research. By investigating LGALS8's role in specific diseases, researchers aim to elucidate its contributions to disease progression and identify potential biomarkers for diagnosis or novel targets for intervention.
