Analytical Data
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Gene name
Galectin-7/LGALS7
- Application
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Alternative Names
Galectin-7/LGALS7, Human (His)
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_002298.1
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Expression Region
S2-F136
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Protein Length
Full Length of Mature Protein
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Molecular Weight
Predicted band size: 17.2 kDa; Observed band size: 18 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-7, also known as LGALS7, is a member of the galectin family of proteins, which are characterized by their ability to bind β-galactosides and play crucial roles in various physiological and pathological processes. Found predominantly in the epidermis, Galectin-7 is implicated in cellular functions such as apoptosis, cell adhesion, and immune responses, making it a key player in skin biology and disease. Studies have shown that Galectin-7 is overexpressed in several cancers and inflammatory conditions, indicating its potential as a biomarker and therapeutic target. The recombinant protein of Galectin-7 is generated using techniques such as recombinant DNA technology, allowing for the production of large quantities of pure protein for further investigation. Researchers aim to elucidate its structure-function relationships and interaction networks to understand its role in cellular mechanisms better. Additionally, Galectin-7's involvement in processes like wound healing and keratinocyte differentiation highlights its significance in skin health and disease management. Investigating the recombinant form of Galectin-7 can provide insights into its biological activity and therapeutic potential, opening avenues for developing treatments for skin-related disorders and cancers where this protein is dysregulated. Understanding the nuances of Galectin-7 will enhance our ability to harness its biological properties for biomedical applications, emphasizing the importance of this recombinant protein in current scientific research.
