Analytical Data
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Gene name
gelE
- Application
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Alternative Names
Coccolysin
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Species
Enterococcus faecalis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q833V7
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Expression Region
193-510aa
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Molecular Weight
50.5 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
GelE, or gelatinase E, is a bacterial enzyme that has garnered significant attention in the field of protein research due to its various applications in biotechnology and medicine. Derived from the pathogenic bacterium *Pseudomonas aeruginosa*, GelE plays a crucial role in the degradation of extracellular matrix components, facilitating tissue invasion and promoting virulence. Researchers have identified GelE as an essential factor in biofilm formation and chronic infections, making it a target for developing novel therapeutic strategies against drug-resistant bacteria. In addition, GelE's unique enzymatic properties enable it to hydrolyze gelatin and other substrates, positioning it as a valuable tool in biocatalysis and protein engineering. The advancement of recombinant DNA technology has made it possible to express GelE in large quantities, allowing for extensive studies on its structure, function, and potential industrial applications. Understanding the molecular mechanisms of GelE can lead to innovations in drug design, wound healing, and even cancer therapy, as its activity can be harnessed for the selective delivery of therapeutics. Overall, the research on GelE is at the intersection of microbiology, biochemistry, and biotechnology, with the potential to significantly impact both fundamental science and practical applications in health and industry.
