Analytical Data
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Gene name
Horcolin
- Application
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Alternative Names
(Agglutinin)(Mannose-specific lectin)
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Species
Hordeum vulgare
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P82953
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Expression Region
1-146aa
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Molecular Weight
22.6 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
Horcolin, a recombinant protein derived from the Horcolin gene, has garnered significant attention in recent years due to its potential therapeutic applications and its role in studying various biological processes. Research into Horcolin began with the identification of its gene sequence, which revealed a unique structure with several conserved domains indicative of functional significance. Initial studies suggested that Horcolin might play a pivotal role in cellular signaling and immune responses, sparking interest in its possible applications in disease treatment. Given its recombinant nature, Horcolin can be produced in controlled environments, allowing for high yields and purity suitable for research and clinical applications. Scientists have focused on elucidating its mechanism of action, exploring how it interacts with other cellular molecules and modulates signaling pathways. Additionally, its expression in model organisms has provided insights into its biological functions. As the understanding of Horcolin expands, research has delved into its potential use in therapeutic interventions for conditions such as autoimmune diseases and cancers, highlighting its relevance in modern biomedical research. The ongoing investigation of Horcolin aims to unlock further insights into its potential benefits and pave the way for future innovations in protein-based therapies.
