Analytical Data
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Gene name
Svs4
- Application
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Alternative Names
Svs4；Svp2；Seminal vesicle secretory Protein 4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18419
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Expression Region
22-113aa
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AA Sequence
KKTKEKFLQSEETVRESFSMGSRGHMSRSSEPEVFVRPQDSIGDEASEEMSSSSSSRRRSKIISSSSDGSNMEGESSYSKRKKSRFSQDALE
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Molecular Weight
17.8 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 Svs4 recombinant protein has gained significant attention in recent years due to its potential applications in biotechnology and medicine. Svs4, a protein derived from the pathogen *Sphingobium yanoikuyae*, plays a critical role in the degradation of toxic compounds, particularly in the context of bioremediation. Its unique structural properties and enzymatic functions make it an attractive candidate for various industrial applications, including environmental cleanup and biosensing. Researchers are particularly interested in understanding the molecular mechanisms underlying its activity and stability, as well as optimizing its production in heterologous systems such as *Escherichia coli*. As the global focus shifts toward sustainable practices and eco-friendly technologies, the exploration of Svs4 and similar proteins holds promise for developing innovative solutions to combat pollution and enhance bioprocess efficiency. By elucidating the structure-function relationships of Svs4, studies aim to harness its capabilities for novel engineering applications, ultimately contributing to a greener future and advancing our understanding of microbial interactions with organic pollutants.
