Analytical Data
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Gene name
RPS6Kb2
- Application
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Alternative Names
RPS6Kb2；FRAP；FRAP1；FRAP2；Serine/threonine-Protein kinase mTOR
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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
Q9UBS0
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Expression Region
1-210aa
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AA Sequence
MAAVFDLDLETEEGSEGEGEPELSPADACPLAELRAAGLEPVGHYEEVELTETSVNVGPERIGPHCFELLRVLGKGGYGKVFQVRKVQGTNLGKIYAMKVLRKAKIVRNAKDTAHTRAERNILESVKHPFIVELAYAFQTGGKLYLILECLSGGELFTHLEREGIFLEDTACFYLAEITLALGHLHSQGIIYRDLKPENIMLSSQGHIKL
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Molecular Weight
50.2 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
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Protein Description
RPS6Kb2, also known as ribosomal protein S6 kinase B2, is a key serine/threonine kinase that plays a crucial role in cell growth, proliferation, and survival by modulating various signaling pathways, particularly the mTOR (mechanistic target of rapamycin) pathway. This protein is part of the broader family of S6 kinases, which are activated in response to growth factors and nutrient availability, influencing protein synthesis and cellular metabolism. Research surrounding RPS6Kb2 has gained momentum due to its implications in various physiological processes and diseases, including cancer, obesity, and metabolic disorders. Studies have shown that dysregulation of RPS6Kb2 can lead to altered cell signaling and contribute to tumorigenesis. Furthermore, the protein is involved in the regulation of glucose homeostasis and insulin signaling, making it a potential target for therapeutic interventions in metabolic diseases. Despite the advancements made in understanding RPS6Kb2's molecular function, the precise mechanisms by which it exerts its effects in different cellular contexts remain to be fully elucidated. Ongoing research aims to explore the role of RPS6Kb2 in cellular response to stress, its interaction with other signaling networks, and its potential as a biomarker or therapeutic target. Understanding the biological functions and regulatory mechanisms of RPS6Kb2 is essential for developing novel strategies to combat diseases associated with its dysregulation, thereby offering insights into its potential applications in clinical settings.
