Analytical Data
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Gene name
ESA
- Application
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Species
Eucheuma serra
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P84331
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Expression Region
1-268aa
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Molecular Weight
35.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 Escherichia coli signal peptide proteins, commonly referred to as ESA (Escherichia coli Signal Peptide and Antibody), has gained significant attention in the field of biotechnology and bioengineering. Signal peptides play a crucial role in protein translocation, guiding nascent polypeptides through cellular membranes and into the extracellular environment or specific organelles. Understanding the mechanisms and structures of these signal peptides is essential for developing more efficient recombinant protein production systems. The use of E. coli as a host for protein expression offers advantages such as rapid growth rates, well-established genetic manipulation techniques, and relatively low production costs. However, challenges remain in the proper folding and post-translational modification of proteins expressed in prokaryotic systems. The research into ESA focuses on optimizing the signal peptidase cleavage process, improving protein yield and solubility, and enhancing the functionality of the target proteins. Moreover, the study of these proteins can lead to advancements in therapeutic protein production, vaccine development, and the creation of novel biomaterials. By elucidating the structure-function relationships of signal peptides and their interactions with the translocation machinery, researchers aim to create engineered E. coli strains tailored for specific biotechnological applications. Overall, ESA research represents a vital intersection of microbiology, protein chemistry, and industrial biotechnology with significant implications for both academic research and commercial applications.
