Analytical Data
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Gene name
STS
- Application
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Alternative Names
STS；ARSC1；Steryl-sulfatase
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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
P08842
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Expression Region
1-583aa
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AA Sequence
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNGCFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQTLPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
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Molecular Weight
65.4 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
STS (Staphylococcal nuclease and Tudor domain containing protein) is a multifunctional protein that has garnered significant attention in recent years due to its diverse roles in cellular processes, including RNA metabolism, DNA repair, and protein interactions. The study of STS arose from the need to understand the intricate regulatory mechanisms governing gene expression and cellular stress responses in various organisms. Researchers have identified STS as a potential biomarker for certain diseases and as a target for therapeutic interventions, particularly in the context of cancer and microbial infections. Advanced techniques such as X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy have enabled scientists to elucidate the structural and functional properties of STS, revealing insights into its interaction with nucleic acids and other proteins. Furthermore, the ability to engineer STS into recombinant forms has opened new avenues for biomedical research and biotechnology applications. By harnessing the unique characteristics of STS, researchers aim to develop novel strategies for manipulating gene expression and enhancing the efficacy of existing treatments, ultimately contributing to the advancement of precision medicine and the development of innovative therapeutic solutions. As the understanding of STS and its biological significance expands, it is anticipated that future studies will continue to uncover novel roles and applications for this intriguing protein, thus underscoring its importance in the landscape of molecular biology and medicine.
