Analytical Data
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Gene name
DEFB116
- Application
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Alternative Names
DEFB116；DEFB16;Beta-defensin 116
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Species
Human
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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
Q30KQ4
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Expression Region
24-102aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI
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Molecular Weight
12 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
DEFB116, a member of the defensin family, is a human antimicrobial peptide encoded by the DEFB1 gene. This protein has garnered interest due to its potential role in the immune response, particularly in the context of infections and inflammatory diseases. Research has shown that DEFB116 exhibits antimicrobial activity against a broad spectrum of pathogens, including bacteria, fungi, and viruses, by disrupting microbial membranes and neutralizing harmful agents. Its expression is often upregulated in response to inflammatory stimuli, suggesting that it plays a crucial role in host defense mechanisms. Furthermore, DEFB116 has been linked to various physiological processes, including wound healing and the regulation of immune responses, highlighting its potential as a therapeutic target. Ongoing studies aim to elucidate the precise mechanisms of action of DEFB116, its interactions with other immune components, and its implications in health and disease. Understanding the functional characteristics and the biochemical properties of DEFB116 could pave the way for novel approaches in developing antimicrobial therapies and enhancing innate immunity.
