Analytical Data
-
Gene name
DEFb113
- Application
-
Alternative Names
DEFb113；DEFB13；Beta-defensin 113
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q30KQ7
-
Expression Region
17-82aa
-
AA Sequence
GPSV PQKKTREVAE RKRECQLVRG ACKPECNSWE YVYYYCNVNP CCAVWEYQKP IINKITSKLH QK
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DEFb113 is a member of the defensin protein family, known for its role in innate immunity, particularly in plants and various animals. These small, cationic peptides exhibit antimicrobial properties, providing a first line of defense against pathogens. The study of DEFb113 has gained prominence due to its potential application in developing novel antimicrobial agents and enhancing disease resistance in crops. Recent research indicates that DEFb113 possesses broad-spectrum antibacterial and antifungal activities, making it a promising candidate for biotechnological applications. Additionally, understanding the structural and functional mechanisms of DEFb113 could shed light on the evolution of immune responses in organisms. The exploration of this protein not only offers insights into plant immunology but also into potential therapeutic strategies for combating antibiotic resistance in human pathogens. As global health challenges increase, exploring the use of such natural peptides could lead to innovative solutions in both agriculture and medicine.
