Analytical Data
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Gene name
DEFB129
- Application
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Alternative Names
Beta-defensin 29 Defensin, beta 129
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Species
Human
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Source
Yeast
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Tag
C- His-Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H1M3
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Expression Region
20-183aa
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Molecular Weight
21.8 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
Defensin beta 129 (DEFB129) is a member of the beta-defensin family, which plays a crucial role in the innate immune response. It is primarily expressed in human epithelial tissues, including the skin, respiratory tract, and gastrointestinal system. The unique antimicrobial properties of DEFB129 make it a subject of interest in research aimed at understanding its role in host defense against pathogens. Studies have shown that DEFB129 exhibits antibacterial, antifungal, and antiviral activities, indicating its potential as a therapeutic agent in combating infections. Additionally, its involvement in modulating inflammation and promoting wound healing highlights its relevance in various clinical conditions. The recombinant expression of DEFB129 has enabled researchers to produce this protein in sufficient quantities for detailed analysis of its structure-function relationship and mechanism of action. Investigating the potential applications of DEFB129 in drug development, particularly in the context of increasing antibiotic resistance, is of significant importance. Overall, the study of DEFB129 recombinant protein offers valuable insights into the development of novel therapeutic strategies to enhance immune responses and fight infections.
