Analytical Data
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Gene name
LGALSL
- Application
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Alternative Names
LGALSL;GRP;Galectin-related Protein
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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
Q3ZCW2
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMAGSVADSDAVVKLDDGHLNNSLSSP VQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDS EDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRV EILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG
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Molecular Weight
22 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
LGALSL (Lactate Dehydrogenase A-Like Protein) is a recently identified protein that has gained attention due to its potential role in various biological processes, including cellular metabolism and cancer progression. The study of LGALSL is rooted in the broader field of protein research, which seeks to understand how proteins function, interact, and contribute to physiological processes. Researchers have found that LGALSL may have similarities to lactate dehydrogenases, enzymes that are critical in the conversion of pyruvate to lactate during anaerobic respiration. Given that many cancer cells rely on anaerobic glycolysis for energy production, exploring LGALSL's function could provide insights into metabolic reprogramming in tumors. Additionally, preliminary studies suggest that LGALSL may be implicated in immune responses and cell signaling pathways, raising questions about its potential as a biomarker for disease or a therapeutic target. Overall, the investigation into LGALSL is part of a larger effort to delineate the intricate networks of proteins that orchestrate cellular function, with implications for understanding disease mechanisms and developing novel treatment strategies.
