Analytical Data
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Gene name
Tachylectin
- Application
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Alternative Names
Lectin L10c
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Species
Tachypleus tridentatus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q27084
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Expression Region
20-255aa
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Molecular Weight
42.8 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
Tachylectins are a group of lectins originally identified in the horseshoe crab (Limulus polyphemus) known for their ability to bind to specific carbohydrates and play a crucial role in the innate immune response. Due to their unique properties, including antimicrobial activity and the ability to recognize pathogen-associated molecular patterns, tachylectins have garnered significant interest in biomedical research. The recombinant production of tachylectin proteins in various expression systems allows for in-depth studies of their structure-function relationships and potential therapeutic applications. Understanding the mechanisms by which tachylectins interact with pathogens can lead to advancements in drug development, particularly in the creation of novel antimicrobial agents or immune modulators. Additionally, tachylectins have potential applications in biosensing technologies due to their specificity in binding, making them valuable tools in diagnostics and clinical research. Studies focusing on the recombinant expression, purification, and functional characterization of tachylectin proteins are essential to explore their roles and applications more comprehensively, laying the groundwork for future innovations in treatment and diagnostic strategies against infectious diseases.
