Analytical Data
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Gene name
Defb4
- Application
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Alternative Names
Defb4；DEFB102；DEFB2；DEFB4；Defensin beta 4A
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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
Q8WTQ1
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Expression Region
23-72aa
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AA Sequence
EFELDRICGYGTARCRKKCRSQEYRIGRCPNTYACCLRKWDESLLNRTKP
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Molecular Weight
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
Related Products
Protein Description
Defb4, also known as the defensin beta 4, is a member of the beta-defensin family of antimicrobial peptides, which play a crucial role in the innate immune response. Identified primarily in epithelial tissues, Defb4 is known to exhibit broad-spectrum antimicrobial activity against bacteria, fungi, and some viruses. Its expression is usually upregulated in response to infections or inflammatory conditions, highlighting its importance in host defense mechanisms. Recent studies have revealed that Defb4 not only functions as an antimicrobial agent but also modulates immune cell responses and contributes to wound healing processes. Given the rising concern over antibiotic resistance, research into Defb4 and related peptides has garnered significant attention in the fields of immunology and microbiology. Scientists are exploring the potential of Defb4 as a therapeutic agent, either in its natural form or as a designed recombinant protein, to combat multidrug-resistant infections. Understanding the structure, function, and regulation of Defb4 can provide insights into its mechanisms of action and pave the way for novel therapeutic strategies that exploit its immunomodulatory properties. As further studies are undertaken, Defb4 holds promise not only for developing new antimicrobial therapies but also for enhancing existing treatment protocols against stubborn infections, making it a focal point of current biomedical research.
