Analytical Data
-
Gene name
isaA
- Application
-
Alternative Names
isaA；Probable transglycosylase IsaA
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P60157
-
Expression Region
30-233aa
-
AA Sequence
AEVNVDQAHLVDLAHNHQDQLNAAPIKDGAYDIHFVKDGFQYNFTSNGTTWSWSYEAANGQTAGFSNVAGADYTTSYNQGSNVQSVSYNAQSSNSNVEAVSAPTYHNYSTSTTSSSVRLSNGNTAGATGSSAAQIMAQRTGVSASTWAAIIARESNGQVNAYNPSGASGLFQTMPGWGPTNTVDQQINAAVKAYKAQGLGAWGF
-
Molecular Weight
28.8 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
The study of isaA recombinant protein is rooted in its significant role in bacterial physiology and pathogenesis, particularly in the context of the bacterium *Streptococcus pneumoniae*. IsaA, or Inducible ginA, is a protein that has been implicated in the bacteria's ability to evade the host immune response and enhance virulence. Understanding the structure and function of isaA is crucial for deciphering its involvement in disease mechanisms, as well as for potential applications in vaccine development or therapeutic interventions. The interest in recombinant versions of this protein arises from the need to investigate its biochemical properties and interactions within the host, which can provide insights into bacterial behavior and potential vulnerabilities. Researchers employ techniques such as molecular cloning and protein expression systems to produce and characterize isaA, leading to a better understanding of its role in the pathogenicity of *S. pneumoniae*. Ultimately, this research may contribute to efforts aimed at combating infections caused by this significant human pathogen.
