Analytical Data
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Gene name
Defb33
- Application
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Alternative Names
Defb33；Beta-defensin 33
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Species
Mouse
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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
Q30KN3
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Expression Region
21-62aa
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AA Sequence
RKRNSKFRPCEKMGGICKSQKTHGCSILPAECKSRYKHCCRL
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Molecular Weight
24.9 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
Defb33, a member of the defensin protein family, is a small cationic peptide known for its antimicrobial properties, particularly in various vertebrates. Defensins play a crucial role in the innate immune system, providing a first line of defense against a wide range of pathogens, including bacteria, viruses, and fungi. Recent studies have highlighted the importance of Defb33 in immune responses, particularly its ability to modulate inflammation and enhance the activation of immune cells. Research has demonstrated that Defb33 can form intrinsically disordered regions that may be crucial for its antimicrobial activity, suggesting a potential mechanism of action that warrants further investigation. Understanding the structure-function relationship of this protein could lead to the development of novel therapeutic agents, particularly in the face of rising antibiotic resistance. Furthermore, exploration of Defb33's expression patterns and regulation could provide insights into its role under physiological and pathological conditions. As such, Defb33 serves as a promising candidate for further studies aimed at elucidating its potential applications in immunotherapy and disease management.
