Analytical Data
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Gene name
GNA16
- Application
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Alternative Names
gB；GNA16；Guanine nucleotide-binding Protein subunit alpha-15
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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
P30679
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Expression Region
1-374aa
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AA Sequence
MARSLTWRCCPWCLTEDEKAAARVDQEINRILLEQKKQDRGELKLLLLGPGESGKSTFIKQMRIIHGAGYSEEERKGFRPLVYQNIFVSMRAMIEAMERLQIPFSRPESKHHASLVMSQDPYKVTTFEKRYAAAMQWLWRDAGIRAYYERRREFHLLDSAVYYLSHLERITEEGYVPTAQDVLRSRMPTTGINEYCFSVQKTNLRIVDVGGQKSERKKWIHCFENVIALIYLASLSEYDQCLEENNQENRMKESLALFGTILELPWFKSTSVILFLNKTDILEEKIPTSHLATYFPSFQGPKQDAEAAKRFILDMYTRMYTGCVDGPEGSKKGARSRRLFSHYTCATDTQNIRKVFKDVRDSVLARYLDEINLL
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Molecular Weight
60.6kDa
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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
GNA16 is a recombinant protein derived from the Galanthus nivalis agglutinin (GNA) family, known for its potential applications in biochemistry, immunology, and agricultural biotechnology. The study of GNA16 originates from the interest in plant lectins, which are proteins that can bind specifically to carbohydrates, thereby mediating various biological processes such as cell-cell interactions and microbial defense mechanisms. Researchers have focused on GNA16 due to its ability to target specific glycoconjugates, making it a useful tool for studying glycan structures and their roles in biological systems. Additionally, GNA16 has garnered attention for its antifungal and antibacterial properties, positioning it as a candidate for developing novel antimicrobial agents. As antibiotic resistance becomes a growing global concern, harnessing the natural capabilities of plant-derived proteins like GNA16 offers a promising avenue for finding alternative therapeutic solutions. Furthermore, the recombinant expression of GNA16 allows for large-scale production, facilitating extensive research into its structural properties and functional mechanisms. The ongoing studies not only enhance our understanding of plant lectin biology but also explore the potential of GNA16 in agricultural applications, such as improving crop resistance to pathogens. Overall, GNA16 serves as an intriguing subject of investigation in multiple fields, highlighting the intersection of plant biotechnology and modern medicine.
