Analytical Data
-
Gene name
plnA
- Application
-
Species
Lactobacillus plantarum
-
Source
E. coli
-
Tag
N- His-SUMO & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P80214
-
Expression Region
26-48aa
-
Molecular Weight
18.7 kDa
-
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
The study of plnA recombinant protein has gained significant attention due to its potential applications in various biotechnological and therapeutic contexts. PlnA, derived from certain bacterial species, encodes a protein known for its antimicrobial properties, particularly against Gram-positive bacteria. Its unique mechanism of action, involving pore formation in bacterial membranes, makes it a promising candidate for the development of new antimicrobial agents in the face of rising antibiotic resistance. Research has focused on the cloning, expression, and purification of plnA to better understand its structure-function relationship and enhance its efficacy. Moreover, recombinant techniques allow for the generation of modified variants of plnA that can potentially improve stability, specificity, or efficacy. These efforts are complemented by studies investigating the protein's safety profile and its behavior in various biological systems, ensuring that any future applications as therapeutic agents are both effective and safe. The cumulative findings from plnA research not only pave the way for innovative antimicrobial therapies but also deepen our understanding of host-pathogen interactions, providing insights that could be leveraged in broader biomedical applications.
