Analytical Data
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Gene name
Serralysin
- Application
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Alternative Names
(Extracellular metalloproteinase)(Serratiopeptidase)(Serrapeptase)(Serrapeptidase)(Zinc proteinase)
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Species
Serratia marcescens
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07268
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Expression Region
17-487aa
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Molecular Weight
56.4 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
Serralysin, a metalloproteinase enzyme originally derived from the bacterium *Serratia marcescens*, has garnered significant attention in the field of biotechnology and biomedicine due to its unique enzymatic properties and potential applications. This enzyme is known for its ability to degrade various extracellular matrix components, making it a valuable tool in tissue remodeling and wound healing studies. Researchers have been exploring the recombinant production of serralysin to enhance its availability and activity for various applications, including cancer research, where its proteolytic activity may help in understanding tumor progression and metastasis. Additionally, serralysin's role in bacterial virulence has stimulated interest in developing novel therapeutic strategies to combat infections caused by *Serratia marcescens* and related pathogens. Recent advancements in recombinant DNA technology have facilitated the efficient expression and purification of serralysin, allowing for detailed characterization of its structure-function relationships and the development of engineered variants with improved properties. Overall, the study of recombinant serralysin holds great promise for advancing both basic research and practical applications in medicine and biotechnology.
