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Cell Signaling Technology Inc phospho s6k1
Phospho S6k1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 2478 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/phospho+s6k1/Phospho-4E-BP1+(Thr37%2F46)+Rabbit+mAb/pm41932558-155-13-14
Average 96 stars, based on 2478 article reviews

phospho s6k1 - by Bioz Stars, 2026-10

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Article Title: Targeting the akt/mtor signaling pathway by maprotiline leads to tumor suppression in T-cell lymphoma.
Article Snippet: The primary antibodies including AKT (4691), phospho-AKT (p-AKT) (4060), mTOR (2983), phospho-mTOR (p-mTOR) (5536), caspase-3 (9662), cleaved caspase-3 (9664), cleaved PARP (5625), phospho-S6K1 (9234), S6K1 (9202), phospho-4EBP1 (2855), 4EBP1 (9644) and GAPDH (5174) were purchased from Cell Signaling Technology (Massachusetts, USA).

Article Title: Targeting the akt/mtor signaling pathway by maprotiline leads to tumor suppression in T-cell lymphoma
Article Snippet: The primary antibodies including AKT (4691), phospho-AKT (p-AKT) (4060), mTOR (2983), phospho-mTOR (p-mTOR) (5536), caspase-3 (9662), cleaved caspase-3 (9664), cleaved PARP (5625), phospho-S6K1 (9234), S6K1 (9202), phospho-4EBP1 (2855), 4EBP1 (9644) and GAPDH (5174) were purchased from Cell Signaling Technology (Massachusetts, USA).

Article Title: Effects of Graded Levels of Calorie Restriction XXI: Impact of Short-term Graded Restriction on Gene Expression Profiles of Stomach and Skeletal Muscle.
Article Snippet: Ac ce pte d M an us cri pt Calorie restriction (CR) extends lifespan and prevents several aging related diseases.. During short-term restriction, we previously showed that lean tissues generally decrease in size, but the alimentary tract (especially the stomach) grows.. To illuminate pathway alterations in these contrasting tissues we compared gene expression profiles (bulk RNAseq) of the skeletal muscle and stomach, in the same male C57BL/6J mice exposed to 3 months of graded CR (0- 40%).

Western Blot:

Article Title: YAP promotes global mRNA translation to fuel oncogenic growth despite starvation
Article Snippet: .. Antibodies against the following antigens were used for immunoblot analysis: puromycin (Kerafast, EQ0001), FLAG (Sigma-Aldrich, F3165), YAP/TAZ (Cell Signaling Technology, #8418), YAP (Cell Signaling Technology, #14074), TEAD4 (Abcam, ab58310), CYR61 (Santa Cruz Biotechnology, sc-13100), DDIT4 (Novus Biologicals, NBP1-22966), mTOR (Cell Signaling Technology, #2972), phospho-S6 (Cell Signaling Technology, #2211), S6 (Cell Signaling Technology, #2217), phospho-4E-BP1 (Cell Signaling Technology, #2855), 4E-BP1 (Cell Signaling Technology, #9644), phospho-ERK (Cell Signaling Technology, #9101), ERK1/2 (Cell Signaling Technology, #4695), phospho-S6K1 (Cell Signaling Technology, #9205), S6K1 (Cell Signaling Technology, #9202), phospho-AKT (Cell Signaling Technology, #4060 and #4056), AKT2 (Cell Signaling Technology, #3063), eIF4E (Santa Cruz Biotechnology, sc-9976), PABP-C1 (Abcam, ab21060), phospho-paxillin (Cell Signaling Technology, #2541), phospho-p38 (Cell Signaling Technology, #4511), and vinculin (Cell Signaling Technology, #13901). ..

Article Title: YAP promotes global mRNA translation to fuel oncogenic growth despite starvation.
Article Snippet: .. Antibodies against the following antigens were used for immunoblot analysis: puromycin (Kerafast, EQ0001), FLAG (Sigma-Aldrich, F3165), YAP/ TAZ (Cell Signaling Technology, #8418), YAP (Cell Signaling Technology, #14074), TEAD4 (Abcam, ab58310), CYR61 (Santa Cruz Biotechnology, sc-13100), DDIT4 (Novus Biologicals, NBP1-22966), mTOR (Cell Signaling Technology, #2972), phospho-S6 (Cell Signaling Technology, #2211), S6 (Cell Signaling Technology, #2217), phospho-4E-BP1 (Cell Signaling Technology, #2855), 4E-BP1 (Cell Signaling Technology, #9644), phosphoERK (Cell Signaling Technology, #9101), ERK1/2 (Cell Signaling Technology, #4695), phospho-S6K1 (Cell Signaling Technology, #9205), S6K1 (Cell Signaling Technology, #9202), phospho-AKT (Cell Signaling Technology, #4060 and #4056), AKT2 (Cell Signaling Technology, #3063), eIF4E (Santa Cruz Biotechnology, sc-9976), PABP-C1 (Abcam, ab21060), phospho-paxillin (Cell Signaling Technology, #2541), phospho-p38 (Cell Signaling Technology, #4511), and vinculin (Cell Signaling Technology, #13901). ..

Phospho-proteomics:

Article Title: Inhibition of autophagy enhances the sensitivity of ciclopirox olamine in human chronic myelogenous leukemia K562 cells
Article Snippet: Antibodies of LC3 (Cell Signaling Technology, MA, USA) and p62 (Santa Cruz Biotechnologies, CA, USA) were used to detect the expression of autophagy biomarkers, LC3 and p62. .. Antibodies of phospho-S6K1 (T389), S6K1, phospho-S6 (S235/236), 4E-BP1, phospho-4E-BP1 (S65), phospho-ULK1 (S555), phospho-ULK1 (S757), phospho-ACC (S79) and ACC, which were purchased from Cell Signaling Technology (Boston, MA, USA), were used to determine the phosphorylation and the total protein expression level of the key proteins in AMPK-ULK1 and mTORC1-ULK1 signaling pathways. .. Antibodies of PARP, caspase-9 and cleaved caspase-3 (Cell Signaling Technology, MA, USA) were used to detect the cleavage of PARP, caspase-9 and caspase-3, which are critical initiator and executioner of apoptosis. β-actin antibody, the secondary antibodies of anti-Mouse IgG-Peroxidase (A9044) and anti-Rabbit IgG-Peroxidase (A0545) were from Sigma-Aldrich (Saint-Louis, MO, USA).

Expressing:

Protein-Protein interactions:

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(A) MTORC1 and AMPK activity is influenced by amino acids and glucose, respectively, and regulate ULK1 activity, which induces autophagy. (B-E) U2OS cells were treated with full media (FM), FM lacking glucose (-Glc), or FM lacking amino acids (-aa) for the indicated times and cell lysates analyzed by immunoblot for ACC, total and phosphorylated at S79 (B, D) , and S6K1 phosphorylated at T389 and actin as a loading control (C, E) . Immunoblots were quantified and signal normalized to total ACC (for D) or actin loading control (for E) plotted. Symbols represent mean of 3 independent experiments and bars are s.e.m. (F-I) Monoclonal U2OS cell lines expressing DFCP1 (F) , WIPI2B (G) , WIPI1 (H) , or ATG5 ( I ) were treated with FM (blue), -Glc (green), or -aa media (red) for 6 hours and subjected to live-cell fluorescent imaging. GFP-puncta (objects) for each reporter were quantified from single cells. Trajectories include mean objects per cell (symbols); bars represent 95% CI. (J-K) GFP-LC3B objects were quantified from cells treated with FM, -aa, or -Glc in the presence of BafA1 (to prevent lysosome degradation) or a vehicle control in 2 hour increments (J) . The number of GFP-LC3 puncta synthesized (solid symbols) and degraded (open symbols) from time 0 min was calculated and plotted. The dashed lines demarcate where individual datasets were collected and data stitched together. Trajectories include mean puncta per cell (symbols); bars represent standard deviation.

Journal: PLOS One

Article Title: Quantitative and temporal analysis of autophagy: Differential Response to amino acid and glucose starvation

doi: 10.1371/journal.pone.0340957

Figure Lengend Snippet: (A) MTORC1 and AMPK activity is influenced by amino acids and glucose, respectively, and regulate ULK1 activity, which induces autophagy. (B-E) U2OS cells were treated with full media (FM), FM lacking glucose (-Glc), or FM lacking amino acids (-aa) for the indicated times and cell lysates analyzed by immunoblot for ACC, total and phosphorylated at S79 (B, D) , and S6K1 phosphorylated at T389 and actin as a loading control (C, E) . Immunoblots were quantified and signal normalized to total ACC (for D) or actin loading control (for E) plotted. Symbols represent mean of 3 independent experiments and bars are s.e.m. (F-I) Monoclonal U2OS cell lines expressing DFCP1 (F) , WIPI2B (G) , WIPI1 (H) , or ATG5 ( I ) were treated with FM (blue), -Glc (green), or -aa media (red) for 6 hours and subjected to live-cell fluorescent imaging. GFP-puncta (objects) for each reporter were quantified from single cells. Trajectories include mean objects per cell (symbols); bars represent 95% CI. (J-K) GFP-LC3B objects were quantified from cells treated with FM, -aa, or -Glc in the presence of BafA1 (to prevent lysosome degradation) or a vehicle control in 2 hour increments (J) . The number of GFP-LC3 puncta synthesized (solid symbols) and degraded (open symbols) from time 0 min was calculated and plotted. The dashed lines demarcate where individual datasets were collected and data stitched together. Trajectories include mean puncta per cell (symbols); bars represent standard deviation.

Article Snippet: Primary antibodies used were Total Acetyl-CoA Carboxylase (ACC; Cell Signaling Technology, 3662), Acetyl-CoA Carboxylase phospho-S79 (Cell Signaling Technology, 11818), S6K1 phospho-T389 (Cell Signaling Technology, 9205), ULK1 phospho-S758 (Cell Signaling Technology, 14202), ULK1 phospho-S556 (Cell Signaling Technology, 5869) and β-actin (Cell Signaling Technology, 3700).

Techniques: Activity Assay, Western Blot, Control, Expressing, Imaging, Synthesized, Standard Deviation

(A) After seeding mouse fibroblasts were cultured in stress conditions for 5 hours with DMSO or SNAP or rapamycin, and p-mTOR, t-mTOR, p-S6K1, t-S6K1, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α and LC-3B II protein levels were detected by immunoblots and quantified using Image J. (B) After seeding mouse lung fibroblasts, cells were cultured in normal conditions for 5 hours with DMSO or SNAP or rapamycin, and p-mTOR, t-mTOR, p-S6K1, t-S6K1, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α and LC-3B protein levels were detected by immunoblots and quantified using Image J. Data in all bar plots are shown as mean ±S.D. and represent three ( A and B ) independent experiments. p values were calculated by one-way ANOVA with Tukey’s multiple comparisons post hoc tests ( A and B ). * p <0.05, ** p <0.01, *** p <0.001; ns, no statistical significance.

Journal: bioRxiv

Article Title: An inducer of snail hibernation causes quiescence and hibernation-like cardioprotection, through metabolic rewiring and autophagy, in mice hearts

doi: 10.64898/2026.01.08.698452

Figure Lengend Snippet: (A) After seeding mouse fibroblasts were cultured in stress conditions for 5 hours with DMSO or SNAP or rapamycin, and p-mTOR, t-mTOR, p-S6K1, t-S6K1, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α and LC-3B II protein levels were detected by immunoblots and quantified using Image J. (B) After seeding mouse lung fibroblasts, cells were cultured in normal conditions for 5 hours with DMSO or SNAP or rapamycin, and p-mTOR, t-mTOR, p-S6K1, t-S6K1, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α and LC-3B protein levels were detected by immunoblots and quantified using Image J. Data in all bar plots are shown as mean ±S.D. and represent three ( A and B ) independent experiments. p values were calculated by one-way ANOVA with Tukey’s multiple comparisons post hoc tests ( A and B ). * p <0.05, ** p <0.01, *** p <0.001; ns, no statistical significance.

Article Snippet: Antibody dilution was 1:1000 for the following immunoblots: p-Rb ser807/811 (Cell Signaling Technology, 8516), Rb (Invitrogen, SY63-03), p-CDK2 Thr160 (Cell Signaling Technology, 2561), t-CDK2 (Abcam, ab32147), β-Actin (Cell Signaling Technology, 3700), t-AMPK (Cell Signaling Technology, 5831), p-AMPK Thr172 (Cell Signaling Technology, 2535), AKT (Cell Signaling Technology, 9272), p-AKT Ser473 (Cell Signaling Technology, 9271), t-S6K1 (Cell Signaling Technology, 2708), and p-S6K1 Thr389 (Cell Signaling Technology, 9205), p-PDHE1α ser232 (Millipore Sigma, AP1063), p-PDHE1α ser300 (Millipore Sigma, AP1064), t-PERK (Cell Signaling Technology, 3192), p-PERK Thr982 (Invitrogen, PA5-40294), ATF6 (Abcam, ab37149), LC3B (Cell Signaling Technology, 2775), cleaved caspase-3 (Cell signaling Technology, 9664), t-mTOR (Cell Signaling Technology, 2983), p-mTOR ser2448 (Cell Signaling Technology, 5536), Ki67 (Abcam, ab16667), p-eIF2α Ser51 (Cell Signaling Technology, 9721), t-eIF2α (Cell Signaling Technology, 5324), Custom p-PDK1 Thr344 (generated by Neobiolab), t-PDK1 (Abcam, ab110025), LDHA (Cell Signaling Technology, 2012), p-JNK Thr183/Tyr185 (Cell Signaling Technology, 9251), t-JNK (Cell Signaling Technology, 3708), α-Tubulin (Cell Signaling Technology, 2144), NHERF-1 (Santa Cruz Biotechnology, sc-271552).

Techniques: Cell Culture, Western Blot

$(A) In vitro IR model: after seeding, mouse cardiomyocytes were cultured in stress conditions for 3 hours with DMSO or SNAP and returned to normal environment without DMSO or SNAP for another 0.5 hours. (B) p-AMPK, t-AMPK, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α, LC3B and cleaved caspase-3 protein levels were detected by immunoblots and quantified with Image J. (C) Representative live images of TMRM and MitoSOX staining of cardiomyocytes after reoxygenation for 0.5 hours (Scale bar: 20 μm) and quantification of fluorescence intensity. (D) Representative immunofluorescence images of citric synthase and p-Akt in cardiomyocytes after 1 hr of ischemic stress (Scale bar: 20 μm), with an increased mitochondrial p-Akt signal with DMSO, diminished by SNAP. (E) Cytosol and mitochondrial fractionation in cardiomyocytes after 1 hour stress, and PHLPP1, NHERF-1, p-AKT, t-AKT, p-PDHE1α Ser300 , t-PDHE1α, PDK1 and LDHA protein levels detected by immunoblots (low and high exposure) and quantified with Image J. The mitochondrial enzyme PDH also served as a marker for mitochondria and the cytosolic enzyme LDH as a cytoplasm marker. Note that the PHLPP1 p-AKT levels increased in the mitochondrial fraction with stress and the mitochondrial, but not cytoplasmic p-AKT, was decreased by SNAP. (F) Protocol for the experiments with cardiomyocytes lacking PDH: after separately seeding αMHC-MerCreMer and Pdha1 Cardiac-/- mouse cardiomyocytes, cells were cultured in stress conditions for 3 hours with DMSO or SNAP and returned to a normal environment without DMSO or SNAP for another 0.5 hours. (G) Measured OCR (Seahorse XF24 Extracellular Flux Analyzer) and calculated SRC (max OCR by FCCP minus min OCR by oligomycin). (H) Cardiomyocyte contractility (cell shortening) after reoxygenation. (I to J), After reoxygenation, ATP ( I ) and acetyl CoA ( J ) levels in cardiomyocytes were measured by HPLC/MS/MS. (K) p-AKT, t-AKT, p-PDHE1α, t-PDHE1α, p-S6K1, t-S6K1 and LC-3B protein levels were detected by immunoblots and quantified with Image J. Data in all bar plots are shown as mean ± S.D. and represent at least three ( C , D , G, H, I and J ) biological replicates per group and three ( B, E and K ) independent experiments. p values were calculated by one-way ANOVA with Tukey’s multiple comparisons post hoc tests ( B , C , E, G, H, I, J and K ). * p <0.05, ** p < 0.01, *** p <0.001; ns, no statistical significance.$

Journal: bioRxiv

Article Title: An inducer of snail hibernation causes quiescence and hibernation-like cardioprotection, through metabolic rewiring and autophagy, in mice hearts

doi: 10.64898/2026.01.08.698452

Figure Lengend Snippet: (A) In vitro IR model: after seeding, mouse cardiomyocytes were cultured in stress conditions for 3 hours with DMSO or SNAP and returned to normal environment without DMSO or SNAP for another 0.5 hours. (B) p-AMPK, t-AMPK, p-AKT, t-AKT, p-PDHE1α, t-PDHE1α, LC3B and cleaved caspase-3 protein levels were detected by immunoblots and quantified with Image J. (C) Representative live images of TMRM and MitoSOX staining of cardiomyocytes after reoxygenation for 0.5 hours (Scale bar: 20 μm) and quantification of fluorescence intensity. (D) Representative immunofluorescence images of citric synthase and p-Akt in cardiomyocytes after 1 hr of ischemic stress (Scale bar: 20 μm), with an increased mitochondrial p-Akt signal with DMSO, diminished by SNAP. (E) Cytosol and mitochondrial fractionation in cardiomyocytes after 1 hour stress, and PHLPP1, NHERF-1, p-AKT, t-AKT, p-PDHE1α Ser300 , t-PDHE1α, PDK1 and LDHA protein levels detected by immunoblots (low and high exposure) and quantified with Image J. The mitochondrial enzyme PDH also served as a marker for mitochondria and the cytosolic enzyme LDH as a cytoplasm marker. Note that the PHLPP1 p-AKT levels increased in the mitochondrial fraction with stress and the mitochondrial, but not cytoplasmic p-AKT, was decreased by SNAP. (F) Protocol for the experiments with cardiomyocytes lacking PDH: after separately seeding αMHC-MerCreMer and Pdha1 Cardiac-/- mouse cardiomyocytes, cells were cultured in stress conditions for 3 hours with DMSO or SNAP and returned to a normal environment without DMSO or SNAP for another 0.5 hours. (G) Measured OCR (Seahorse XF24 Extracellular Flux Analyzer) and calculated SRC (max OCR by FCCP minus min OCR by oligomycin). (H) Cardiomyocyte contractility (cell shortening) after reoxygenation. (I to J), After reoxygenation, ATP ( I ) and acetyl CoA ( J ) levels in cardiomyocytes were measured by HPLC/MS/MS. (K) p-AKT, t-AKT, p-PDHE1α, t-PDHE1α, p-S6K1, t-S6K1 and LC-3B protein levels were detected by immunoblots and quantified with Image J. Data in all bar plots are shown as mean ± S.D. and represent at least three ( C , D , G, H, I and J ) biological replicates per group and three ( B, E and K ) independent experiments. p values were calculated by one-way ANOVA with Tukey’s multiple comparisons post hoc tests ( B , C , E, G, H, I, J and K ). * p <0.05, ** p < 0.01, *** p <0.001; ns, no statistical significance.

Techniques: In Vitro, Cell Culture, Western Blot, Staining, Fluorescence, Immunofluorescence, Fractionation, Marker, Tandem Mass Spectroscopy

By resetting the balance of the fuel supply/demand sensors mTOR and AMPK, SNAP puts cells into the stress-resistant hibernation zone under demand>supply (IR) states, while in its absence, cells undergo ischemic damage. Bottom : Under IR the translocation of PHLPP1 and p-AKT to both the cytoplasm and mitochondria enables SNAP to dephosphorylate p-S6K1 in the cytoplasm and p-Akt in the mitochondria, thereby reducing apoptosis and mROS induced ER stress as well as enhancing autophagy. AKT can be activated in hypoxia by the low glucose and oxygen while in reperfusion by ROS originating either in the membrane or mitochondria. This dual inhibition by SNAP is the basis of resetting the balance between AMPK and mTOR.

Journal: bioRxiv

Article Title: An inducer of snail hibernation causes quiescence and hibernation-like cardioprotection, through metabolic rewiring and autophagy, in mice hearts

doi: 10.64898/2026.01.08.698452

Figure Lengend Snippet: By resetting the balance of the fuel supply/demand sensors mTOR and AMPK, SNAP puts cells into the stress-resistant hibernation zone under demand>supply (IR) states, while in its absence, cells undergo ischemic damage. Bottom : Under IR the translocation of PHLPP1 and p-AKT to both the cytoplasm and mitochondria enables SNAP to dephosphorylate p-S6K1 in the cytoplasm and p-Akt in the mitochondria, thereby reducing apoptosis and mROS induced ER stress as well as enhancing autophagy. AKT can be activated in hypoxia by the low glucose and oxygen while in reperfusion by ROS originating either in the membrane or mitochondria. This dual inhibition by SNAP is the basis of resetting the balance between AMPK and mTOR.

Techniques: Translocation Assay, Membrane, Inhibition

Regulatory effect of Notch/mTOR on the developmental process of PFs in zebrafish. ( A ) qRT-PCR to detect the expression of notch2 , akt2 , and mtor genes in different types of PFs in zebrafish. ( B ) Immunohistochemistry (IHC) to detect the Notch and mTOR proteins localization in the ovary and expression of different types of PFs of zebrafish; scale bar, 50 μM; ( C , F , I ) Histological observation of the ovary in the treated group with IMR-1, P529, and dietary amino acid supplementation; scale bar, 100 μM. ( D ) The hey1 , hey2 , hes , mtor , and s6k1 mRNA levels in the ovary tissues of IMR-1-treated groups. ( E ) The Notch, mTOR, and p-mTOR protein levels were expressed in the ovarian tissues of IMR-1-treated groups. ( G ) The s6k1 and notch mRNA levels were expressed in the ovarian tissues of the P529-treated groups. ( H ) The mTOR, p-mTOR, S6K1, and p-S6K1 protein levels of expression in the ovarian tissues of the P529-treated groups. ( J ) The mtor , s6k1 , and notch mRNA levels of expression in the ovarian tissues of the amino acid addition group. ( K ) The mTOR, p-mTOR, S6K1, P-S6K1, and Notch protein levels were expressed in the ovarian tissues of the amino acid addition group. “*”: p < 0.05; “**”: p < 0.01; “***”: p < 0.001 ; “****”: p < 0.0001. (means ± SD of relative expression; n = 3 for each group).

Journal: Biology

Article Title: Primary Follicle Paces Fish Ovarian Maturation Developmental Progression via the Enhancement of Notch and mTOR

doi: 10.3390/biology14121752

Figure Lengend Snippet: Regulatory effect of Notch/mTOR on the developmental process of PFs in zebrafish. ( A ) qRT-PCR to detect the expression of notch2 , akt2 , and mtor genes in different types of PFs in zebrafish. ( B ) Immunohistochemistry (IHC) to detect the Notch and mTOR proteins localization in the ovary and expression of different types of PFs of zebrafish; scale bar, 50 μM; ( C , F , I ) Histological observation of the ovary in the treated group with IMR-1, P529, and dietary amino acid supplementation; scale bar, 100 μM. ( D ) The hey1 , hey2 , hes , mtor , and s6k1 mRNA levels in the ovary tissues of IMR-1-treated groups. ( E ) The Notch, mTOR, and p-mTOR protein levels were expressed in the ovarian tissues of IMR-1-treated groups. ( G ) The s6k1 and notch mRNA levels were expressed in the ovarian tissues of the P529-treated groups. ( H ) The mTOR, p-mTOR, S6K1, and p-S6K1 protein levels of expression in the ovarian tissues of the P529-treated groups. ( J ) The mtor , s6k1 , and notch mRNA levels of expression in the ovarian tissues of the amino acid addition group. ( K ) The mTOR, p-mTOR, S6K1, P-S6K1, and Notch protein levels were expressed in the ovarian tissues of the amino acid addition group. “*”: p < 0.05; “**”: p < 0.01; “***”: p < 0.001 ; “****”: p < 0.0001. (means ± SD of relative expression; n = 3 for each group).

Article Snippet: Membranes were blocked with 3–5% skim milk for 1.5 h at room temperature, followed by overnight incubation at 4 °C with the following rabbit monoclonal primary antibodies: Notch (1:1000, AF5296, Affinity Biosciences, Cincinnati, OH, USA), mTOR (1:1000, HA500126 , Huabio, Hangzhou, China), p-mTOR (1:1000, HA721632, Huabio), S6K1 (1:500, HA500095 , Huabio), p-S6K1 (1:1000, 9205S, Cell Signaling Technology, Danvers, MA, USA), α-tubulin (1:1000, ER130905 , Huabio), and β-actin (1:1000, EM21002, Huabio).

Techniques: Quantitative RT-PCR, Expressing, Immunohistochemistry

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