Analytical Data
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Gene name
Galectin 1
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简介
Galectin-1/LGALS1 protein is a β-galactoside-binding lectin that regulates apoptosis, cell proliferation, and differentiation by inhibiting CD45 protein phosphatase. It prevents Lyn kinase dephosphorylation, induces T cell apoptosis as a homodimer, and interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Galectin 1 Protein, Mouse (HEK293, hFc) is the recombinant mouse-derived Galectin 1 protein, expressed by HEK293, with N-hFc labeled tag.
- Application
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Alternative Names
Galectin-1; HLBP14; S-Lac lectin 1; LGALS1; GAL1; GBP; DKFZp686E23103; Galectin 1
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Species
Mouse
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Source
HEK293
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Tag
N-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16045
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Expression Region
A2-E135
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Protein Length
Full Length of Mature Protein
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Molecular Weight
45-52 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-1, a member of the galectin family of proteins, has garnered significant interest in biomedical research due to its multifunctional roles in cellular processes, including cell adhesion, migration, and apoptosis. This β-galactoside-binding lectin is primarily expressed in immune cells, endothelial cells, and various tissues, where it contributes to immune regulation and inflammation modulation. Its involvement in various pathological conditions, such as cancer, autoimmune diseases, and infectious diseases, positions Galectin-1 as a critical player in immune responses, often acting as a potential therapeutic target or biomarker. In cancer, for instance, Galectin-1 can facilitate tumor progression by promoting immune evasion and enhancing angiogenesis. Consequently, the expression and activity of Galectin-1 have become focal points in the study of tumor microenvironments and the development of novel therapeutic strategies. Recombinant Galectin-1 protein production allows for a deeper understanding of its structural and functional properties, enabling researchers to explore its interactions with other biomolecules and assess its potential as a drug target. By generating and characterizing recombinant Galectin-1, researchers aim to elucidate its biological roles and therapeutic applications, paving the way for advancements in treatment strategies for a range of diseases influenced by this pivotal protein.
