Analytical Data
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Gene name
STR1
- Application
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Alternative Names
/
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Species
Rauvolfia serpentina
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P68175
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Expression Region
23-344aa
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Molecular Weight
43.2 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
STR1 recombinant protein has garnered significant attention in the field of molecular biology and biomedicine due to its potential role in various physiological processes and disease mechanisms. STR1, or Serine/Threonine-rich protein 1, is implicated in important cellular functions, including signal transduction and cellular differentiation, making it a valuable target for therapeutic intervention. Research has shown that alterations in the expression or function of STR1 may contribute to the progression of several diseases, such as cancer and neurodegenerative disorders. The recombinant production of STR1 facilitates detailed studies of its structure-function relationship and interaction with other biological molecules, allowing researchers to explore its potential as a biomarker or therapeutic target. Additionally, the availability of STR1 in a purified form aids in high-throughput screening for drug development, enabling the identification of compounds that could modulate its activity. As the understanding of STR1's biological roles expands, it opens up new avenues for clinical applications, including targeted therapy and personalized medicine, underscoring the importance of ongoing research in this area. Thus, the study of STR1 recombinant protein not only enhances our understanding of fundamental biological processes but also paves the way for innovative strategies in disease treatment.
