Analytical Data
-
Gene name
DEFa2
- Application
-
Alternative Names
Defcr2; Defensin-Related Cryptdin-2; Cryptdin-1
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P59665
-
Expression Region
Gln18~Cys94
-
Molecular Weight
38kDa
-
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
DEFa2, also known as Defensin alpha 2, is a member of the defensin family of antimicrobial peptides that play a crucial role in the innate immune response. The study of DEFa2 and its recombinant form has garnered significant attention due to its potential applications in therapeutic interventions and its role in host defense mechanisms. Research indicates that DEFa2 displays antimicrobial properties against a wide range of pathogens, including bacteria, viruses, and fungi, making it a promising candidate for developing new antimicrobial agents, especially in the context of rising antibiotic resistance. Additionally, DEFa2 is implicated in modulating inflammation and immune responses, further highlighting its significance in various pathological conditions. Recent advancements in recombinant DNA technology have enabled the expression and purification of DEFa2, allowing for detailed studies into its structure-function relationships and therapeutic potential. Understanding the biophysical characteristics and mechanisms of action of DEFa2 could lead to novel strategies for enhancing innate immunity or designing new drugs that mimic its functions. Moreover, as researchers explore its role in specific diseases, including infections and inflammatory disorders, DEFa2's profile as a multifunctional peptide continues to evolve, solidifying its importance in both basic and applied biomedical research.
