Recombinant human S6K1 protein (Tagged-His Tag) is a Human Full Length protein, in the 1 to 525 aa range, expressed in Baculovirus infected Sf9, with >85% purity and suitable for SDS-PAGE, FuncS.
M R R R R R R D G F Y P A P D F R D R E A E D M A G V F D I D L D Q P E D A G S E D E L E E G G Q L N E S M D H G G V G P Y E L G M E H C E K F E I S E T S V N R G P E K I R P E C F E L L R V L G K G G Y G K V F Q V R K V T G A N T G K I F A M K V L K K A M I V R N A K D T A H T K A E R N I L E E V K H P F I V D L I Y A F Q T G G K L Y L I L E Y L S G G E L F M Q L E R E G I F M E D T A C F Y L A E I S M A L G H L H Q K G I I Y R D L K P E N I M L N H Q G H V K L T D F G L C K E S I H D G T V T H T F C G T I E Y M A P E I L M R S G H N R A V D W W S L G A L M Y D M L T G A P P F T G E N R K K T I D K I L K C K L N L P P Y L T Q E A R D L L K K L L K R N A A S R L G A G P G D A G E V Q A H P F F R H I N W E E L L A R K V E P P F K P L L Q S E E D V S Q F D S K F T R Q T P V D S P D D S T L S E S A N Q V F L G F T Y V A P S V L E S V K E K F S F E P K I R S P R R F I G S P R T P V S P V K F S P G D F W G R G A S A S T A N P Q T P V E Y P M E T S G I E Q M D V T M S G E A S A P L P I R Q P N S G P Y K K Q A F P M I S K R P E H L R M N L
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed:16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed:16286006). The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B (PubMed:16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed:17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed:15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed:11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:19720745, PubMed:19935711, PubMed:19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed:17936702). The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function (PubMed:17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed:18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed:17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239).
STK14A, RPS6KB1, Ribosomal protein S6 kinase beta-1, S6K-beta-1, S6K1, 70 kDa ribosomal protein S6 kinase 1, Ribosomal protein S6 kinase I, Serine/threonine-protein kinase 14A, p70 ribosomal S6 kinase alpha, P70S6K1, p70-S6K 1, p70 S6 kinase alpha, p70 S6K-alpha, p70 S6KA
Recombinant human S6K1 protein (Tagged-His Tag) is a Human Full Length protein, in the 1 to 525 aa range, expressed in Baculovirus infected Sf9, with >85% purity and suitable for SDS-PAGE, FuncS.
pH: 7
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
Affinity purified.
Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed:16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed:16286006). The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B (PubMed:16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed:17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed:15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed:11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:19720745, PubMed:19935711, PubMed:19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed:17936702). The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function (PubMed:17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed:18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed:17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239).
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.
Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism (PubMed:18925875, PubMed:19085255, PubMed:22017876, PubMed:23429703, PubMed:29236692). Activated by phosphorylation at Thr-252 by PDPK1 (PubMed:19864428, PubMed:9445476). Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (PubMed:17936702).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
S6K1 also known as p70S6K is a serine/threonine kinase involved in protein synthesis. The protein has a molecular weight of approximately 70 kDa. Scientists often examine the presence of S6K1 in various tissues as it is expressed ubiquitously in eukaryotic cells. This kinase plays an instrumental role in the regulation of cell growth proliferation and survival by phosphorylating ribosomal protein S6 and other targets. Researchers explore various cellular contexts where S6K1 activity is implicated due to its widespread expression and function.
S6K1 functions as a downstream effector of the mammalian target of rapamycin (mTOR) complex specifically mTORC1. S6K1 interacts with several protein complexes enhancing its regulatory capacity in cellular activities. It modulates protein synthesis by phosphorylating substrates involved in translation. By controlling these processes S6K1 aids in cell size regulation and energy metabolism which are critical for maintaining cellular homeostasis and adaptation to nutrient availability.
S6K1 plays an essential role in the mTOR signaling pathway a central regulator of cell growth and metabolism. S6K1 functions in close connection with proteins such as mTOR and Raptor within this pathway. Additionally it is involved in the insulin signaling pathway where it works with proteins like insulin receptor substrate (IRS). Both pathways highlight S6K1's role in nutrient sensing and response emphasizing its significance in energy and protein homeostasis.
S6K1 is associated with conditions such as cancer and type 2 diabetes. Dysregulation of S6K1 activity can lead to abnormal cell proliferation contributing to oncogenesis in various cancer types. Specifically altered signaling through pathways involving mTOR and Akt proteins connects S6K1 to cancer progression. In type 2 diabetes S6K1 affects insulin sensitivity where overactive S6K1 signaling leads to insulin resistance. Here interactions with insulin receptor substrate proteins highlight its influence on metabolic disorders underlining its critical role in disease pathology.
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The specific activity was determined to be 89 nmol/min/mg in a kinase assay using S6K synthetic peptide substrate.
SDS-PAGE analysis of ab268834.
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