Analytical Data
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Gene name
Defb33
- Application
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Alternative Names
Defensin, beta 33
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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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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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 is a member of the β-defensin family, which plays a crucial role in the innate immune response. These small cationic peptides are primarily produced by epithelial cells and exhibit antimicrobial activities against a broad spectrum of pathogens, including bacteria, fungi, and viruses. The study of Defb33 has gained importance due to its potential implications in immunology and therapeutic applications. Recent research has suggested that Defb33 not only functions as an antimicrobial agent but also plays a role in modulating the immune response by influencing inflammation and wound healing processes. The understanding of its structure-function relationship has been enhanced through recombinant protein technology, enabling the production of Defb33 in various systems for detailed functional assays. This research has broader implications, particularly in understanding host defense mechanisms and developing novel antimicrobial peptides that could serve as alternatives to conventional antibiotics. Furthermore, alterations in the expression levels of β-defensins, including Defb33, have been linked to various diseases, making it a target of interest in medical research. With the increasing prevalence of antibiotic resistance, the exploration of Defb33 and similar peptides could yield valuable insights and strategies for combating infections and enhancing human health.
