Analytical Data
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Gene name
LGALS13
- Application
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Alternative Names
LGALS13;PLAC8;Galactoside-binding soluble lectin 13
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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
Q9UHV8
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Expression Region
1-139aa
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AA Sequence
MSSLPVPYKL PVSLSVGSCV IIKGTPIHSF INDPQLQVDF YTDMDEDSDI AFRFRVHFGN HVVMNRREFG IWMLEETTDY VPFEDGKQFE LCIYVHYNEY EIKVNGIRIY GFVHRIPPSF VKMVQVSRDI SLTSVCVCN
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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
LGALS13, also known as galectin-13, is a member of the galectin family, which are β-galactoside-binding proteins involved in various biological processes, including cell-cell interaction, inflammation, and immune responses. Research has indicated that LGALS13 plays a significant role in several critical physiological and pathological conditions, such as cancer progression, autoimmune diseases, and infectious diseases. The protein is primarily expressed in immune cells, where it modulates immune responses by influencing the behavior of T cells and macrophages. Furthermore, studies have suggested that LGALS13 may have potential therapeutic applications, particularly in cancer immunotherapy, as it can promote tumor progression by modulating the tumor microenvironment. Understanding the structure and function of recombinant LGALS13 can provide insights into its molecular mechanisms and enhance our ability to manipulate its effects in therapeutic contexts. Thus, the production of recombinant LGALS13 protein has become a focal point of research, aiming to elucidate its biological functions and explore its potential as a biomarker or therapeutic target in various diseases. This recombinant protein serves as a valuable tool for studying its interactions with other biomolecules, evaluating its role in disease models, and developing novel therapeutic strategies that could improve disease outcomes. Overall, LGALS13 remains a promising candidate for further research due to its involvement in crucial biological processes and its potential implications in medical science.
