Analytical Data
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Gene name
STH
- Application
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Alternative Names
STH; Saitohin
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Species
Human
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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
Q8IWL8
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Expression Region
1-128aa
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Molecular Weight
29.7 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
STH recombinant protein research is a burgeoning field focused on the synthesis, characterization, and application of proteins derived from the STH (secreted and membrane-bound proteins) family. This family plays critical roles in various biological processes, including signal transduction, immune responses, and cellular communication. Advances in molecular biology techniques, such as recombinant DNA technology, have enabled scientists to produce these proteins in host systems like bacteria, yeast, or mammalian cells, facilitating their study in controlled environments. The recombinant proteins not only provide insights into the fundamental mechanisms of cellular and molecular biology but also hold potential therapeutic applications. For instance, they could be used in vaccine development, as diagnostic tools, or in targeted therapies for diseases. The ability to manipulate these proteins through genetic engineering also opens avenues for creating modified versions with enhanced stability, specificity, or activity. As research progresses, understanding the functional roles and interactions of STH recombinant proteins will not only expand our knowledge of cellular processes but also pave the way for innovative applications in biotechnology and medicine.
