Analytical Data
-
Gene name
lytA
- Application
-
Alternative Names
N-acetylmuramoyl-L-alanine amidase
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P24556
-
Expression Region
1-481aa
-
Molecular Weight
57.8 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
LytA, a key autolysin enzyme in Streptococcus pneumoniae, plays a crucial role in bacterial cell wall metabolism and contributes to the bacterium's pathogenicity. Understanding LytA's structure and function is essential for developing new therapeutic strategies against pneumococcal infections, which remain a major public health concern despite the availability of vaccines. Research on LytA recombinant proteins has gained traction in recent years, as these proteins can be utilized to investigate the enzyme's active site, substrate specificity, and interaction with other cell wall components. Additionally, LytA recombinant proteins offer potential as vaccine candidates, as they may elicit protective immune responses. Studies have focused on the expression and purification of LytA in various systems, alongside the characterization of its enzymatic activity to uncover its biological significance. As antibiotic resistance continues to rise, targeting virulence factors like LytA presents a promising approach to developing alternative treatments. The ongoing research aims to provide insights into LytA's mechanism of action, paving the way for innovative interventions against Streptococcus pneumoniae and related pathogens.
