Analytical Data
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Gene name
DEFB130
- Application
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Alternative Names
DEFB130；DEFB130；DEFB30；Beta-defensin 130A
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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
Q30KQ2
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Expression Region
23-79aa
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AA Sequence
GVIPGQKQCIALKGVCRDKLCSTLDDTIGICNEGKKCCRRWWILEPYPTPVPKGKSP
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Molecular Weight
8.3 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
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Protein Description
DEFB130, a member of the defensin protein family, plays a crucial role in the innate immune response. Defensins are small cationic peptides that exhibit antimicrobial activity against a broad range of pathogens, including bacteria, fungi, and viruses. DEFB130 is primarily expressed in human epithelial tissues, particularly in the skin and respiratory tract, where it serves as a first line of defense against microbial invasion. Research into DEFB130 has gained traction due to its potential therapeutic applications in treating infections and inflammatory diseases. The recombinant expression of DEFB130 has enabled scientists to study its structural features and functional mechanisms more effectively. By producing this protein in a laboratory setting, researchers can investigate its antimicrobial properties, binding interactions with pathogens, and immunomodulatory effects. Furthermore, understanding the genetic regulation of DEFB130 expression may uncover insights into how variations in this defensin contribute to individual susceptibility to infections and inflammation. The study of DEFB130 also holds promise for the development of novel antimicrobial agents and therapeutic strategies that harness the body’s natural defenses. Given the rising prevalence of antibiotic resistance, DEFB130 and other defensins represent a vital area of research aimed at alternative treatment options that can mitigate infectious diseases while promoting human health.
