Analytical Data
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Gene name
SGK
- Application
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Alternative Names
Serine/threonine-protein kinase Sgk1. EC:2.7.11.1. Serum/glucocorticoid-regulated kinase 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00141
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Expression Region
1-431 aa
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AA Sequence
MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLGFSYAPPTDSFL
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Molecular Weight
73.04 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
SGK (serum/glucocorticoid-regulated kinase) is a family of protein kinases that plays a crucial role in various cellular processes, including cell survival, proliferation, and metabolism. Initially identified due to its regulation by serum and glucocorticoids, SGK has been recognized for its functional similarities to AKT, a key player in the phosphatidylinositol 3-kinase (PI3K) signaling pathway. Research has increasingly focused on the role of SGK in several physiological and pathophysiological contexts, such as tissue growth, insulin signaling, and response to stress. The protein's distinct isoforms—SGK1, SGK2, and SGK3—exhibit unique expression patterns and regulatory mechanisms, further heightening interest in their specific biological roles. Additionally, dysregulation of SGK expression or activity has been implicated in diseases such as cancer, diabetes, and cardiovascular disorders. To better understand these mechanisms, studies on SGK often involve the production and characterization of recombinant SGK proteins, which allows researchers to dissect the molecular functions and interactions of these kinases in vitro and in vivo. This research is not only vital for elucidating the biological significance of SGK in cellular signaling but also holds potential implications for therapeutic interventions targeting SGK pathways in various diseases. Through the development of specific SGK inhibitors or modulators, there is hope for advancing treatment strategies that are more effective and have fewer side effects. Overall, SGK's essential functions in health and disease make it a valuable subject of research in cell biology and medicine.
