Analytical Data
-
Gene name
DEFa5
- Application
-
Alternative Names
DEFa5；DEF5；Defensin alpha 5
-
Species
Mouse
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P28312
-
Expression Region
59-93aa
-
AA Sequence
SKKLICYCRIRGCKRRERVFGTCRNLFLTFVFCCS
-
Molecular Weight
31.2kDa
-
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
DEFa5 is a member of the defensin family of antimicrobial peptides, which are crucial components of the innate immune system. Found predominantly in the skin and various mucosal surfaces, DEFa5 plays a significant role in host defense against a wide range of pathogens, including bacteria, fungi, and viruses. The interest in studying DEFa5, particularly in its recombinant form, has grown due to its potential applications in therapeutic areas, such as wound healing and infection control. Research has revealed that DEFa5 exhibits not only antimicrobial properties but also immunomodulatory effects, enhancing the overall immune response. Additionally, the ability to produce DEFa5 as a recombinant protein allows for large-scale production and purification, facilitating detailed studies on its structure-activity relationship. Understanding the molecular mechanisms underlying DEFa5's function can lead to the development of novel antimicrobial agents and strategies for combating antibiotic resistance. The exploration of DEFa5 also aligns with broader trends in peptide research, emphasizing the significance of natural molecules in drug discovery and development. As we delve deeper into the properties and applications of DEFa5, it holds promise as a key player in future therapeutic innovations in the field of infectious diseases and immunology.
