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anti phospho rps6 antibody (Cell Signaling Technology Inc)

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Cell Signaling Technology Inc anti phospho rps6 antibody
Anti Phospho Rps6 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+rps6/Phospho-S6+Ribosomal+Protein+(Ser240%2F244)+XP+Rabbit+mAb/bio_rxiv__64898__2026__03__27__714790-190-9-13
Average 96 stars, based on 1112 article reviews

anti phospho rps6 antibody - by Bioz Stars, 2026-09

96/100 stars

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Article Title: Cytosolic and ER-associated ribosomes share rRNA 2′-O-methylation landscapes across human cell types
Article Snippet: The following primary antibodies were used: rabbit anti-Calnexin (Cell Signaling Technology, 2679S; 1:1000), mouse anti-GAPDH (Santa Cruz Biotechnology, sc-47724; 1:2000), rabbit anti-Histone H3 (Cell Signaling Technology, 9756; 1:1000), rabbit anti-RPS6 (Cell Signaling Technology, 2217; 1:4000), rabbit anti-RPL10A (RayBiotech, 144-05925; 1:1000), mouse anti-Tuj1 (STEMCELL Technologies, 60092; 1:500), and mouse anti-RPL22 (Santa Cruz Biotechnology, sc-136413; 1:1000).

Article Title: An autism spectrum disorder mutation in Topoisomerase 3β causes accumulation of covalent mRNA intermediates by disrupting metal binding within the zinc finger domain
Article Snippet: Mouse anti-FLAG M2 (Sigma #F3165-1mg), rabbit anti-V5 (Cell Signaling #13202; clone D3H8Q), rabbit anti-Ubiquitin (Cell Signaling #43124; clone E4I2J), rabbit anti-GFP (Cell Signaling #2956; clone D5.1), mouse anti-alpha (α) Tubulin (Sigma #T9026), rabbit anti-RPS6 (Cell Signaling #2217; clone 5G10), rabbit anti-RPL7 (Abcam #ab72550), and rabbit anti-RPS10 (Abcam #ab151550; clone EPR8545) were used at 1:1000 in TBST with 0.02% (w/v) sodium azide.

Article Title: An autism spectrum disorder mutation in Topoisomerase 3β causes accumulation of covalent mRNA intermediates by disrupting metal binding within the zinc finger domain.
Article Snippet: Mouse anti-FLAG M2 (Sigma #F3165-1mg), rabbit anti-V5 (Cell Signaling #13202; clone D3H8Q), rabbit anti-Ubiquitin (Cell Signaling #43124; clone E4I2J), rabbit anti-GFP (Cell Signaling #2956; clone D5.1), mouse anti-alpha ( α) Tubulin (Sigma #T9026), rabbit anti-RPS6 (Cell Signaling #2217; clone 5G10), rabbit anti-RPL7 (Abcam #ab72550), and rabbit anti-RPS10 (Abcam #ab151550; clone EPR8545) were used at 1:1000 in TBST with 0.02% (w/v) sodium azide.

Article Title: Hydrogen sulfide as a potent predator-derived kairomone mediating fear-related responses in mice.
Article Snippet: Primary antibodies were used in specific serum solution overnight at 4 °C: Rabbit anti-CNGA3 (1:800; Lifespan Bioscience), Rabbit anti-rpS6 (1/400; Cell signaling, MA, USA; #5364) and Rabbit anti-cFOS (1/500; ABCAM, Cambridge, UK; #ab190289).

Article Title: Hydrogen sulfide as a potent predator-derived kairomone mediating fear-related responses in mice
Article Snippet: Primary antibodies were used in specific serum solution overnight at 4 °C: Rabbit anti-CNGA3 (1:800; Lifespan Bioscience), Rabbit anti-rpS6 (1/400; Cell signaling, MA, USA; #5364) and Rabbit anti-cFOS (1/500; ABCAM, Cambridge, UK; #ab190289).

Western Blot:

Article Title: A family of lethal exotoxins defined by cell entry via the Attractin receptor
Article Snippet: .. Fractions were additionally analyzed by Western blot with rabbit-anti-RpS6 (Cell Signaling Technology, 2217). .. For in vitro AMPylation, ALFA-Rac1 was obtained by transiently transfecting Drosophila S2 cells with pAc5.1/ALFA-Rac using Effectene, followed by ALFA selector purification and elution with ALFA peptide (Nanotag Biotechnologies).

Incubation:

Article Title: Large increases in resistance training volume do not impair skeletal muscle hypertrophy or anabolic–catabolic molecular signalling in trained individuals
Article Snippet: .. The membranes were incubated overnight at 4°C with the following antibodies at a dilution of 1:1000 in TBST with 5% bovine serum albumin (BSA): rabbit anti-MyHC (cat. no: 64038, Cell Signaling Technology); rabbit anti-polyubiquitin (cat. no: 3933, Cell Signaling Technology); rabbit 20S antibody cocktail (cat. no: PW8155, Enzo Life Sciences); rabbit anti-calpain-1 (cat. no: 2556, Cell Signaling Technology); rabbit anti-calpain-2 (cat. no: 70655, Cell Signaling Technology); rabbit anti-LC3 (cat. no: 2775, Cell Signaling Technology); rabbit anti-FOXO1 (cat. no: 9454, Cell Signaling Technology); rabbit anti-FOXO3 (cat. no: 24975, Cell Signaling Technology); rabbit anti-RPS6 (cat. no: 2217, Cell Signaling Technology); rabbit anti-4EBP1 (cat. no: 9644, Cell Signaling Technology); rabbit anti-phospho-4EBP1 (cat. no: 2855, Cell Signaling Technology); rabbit anti-p62 (cat. no: 5114, Cell Signaling Technology); mouse anti-SKIV2L2 (cat. no: sc-515828, Santa Cruz Technology); mouse anti-G3BP1 (cat. no: sc-365338, Santa Cruz Technology); rabbit anti-p70S6K (cat. no: 9234, Cell Signaling Technology); rabbit anti-phospho-p70S6K (cat. no: 2983, Cell Signaling Technology); rabbit anti-mTOR (cat. no: 5536, Cell Signaling Technology); rabbit anti-phospho-mTOR (cat. no: 2971, Cell Signaling Technology). ..

Immunohistochemistry:

Article Title: Vitamin D Regulates Olfactory Function via Dual Transcriptional and mTOR-Dependent Translational Control of Synaptic Proteins.
Article Snippet: Capillary cartridges (Protein Simple, SM-W004-1), anti-rabbit detectionmodule chemiluminescence (Protein Simple DM-001), anti-mouse detection module chemiluminescence (Protein Simple DM-002), and EZ standard pack (Protein Simple PS-ST01EZ-8) were used according to the manufacturer’s instructions. .. The following antibodies were used (if notmentioned in the immunohistochemistry section): mouse anti-β-actin (1:200, Novus, NB600501), rabbit anti-AKT (1:200, Cell Signaling Technology, 4691), rabbit antip-AKT (1:20, Cell Signaling Technology, 4060), rabbit anti-eIF4E (1:100, Cell Signaling Technology, 2067), rabbit anti-eIF4EBP1 (1:100, Cell Signaling Technology, 9644), rabbit anti-p-eIF4EBP1 (1:200, Cell Signaling Technology, 2855), rabbit anti-eIF4EBP2 (1:20, CST, 2845), rabbit anti-GAPDH (1:5000, Cell Signaling Technology, 5174), mouse anti-gephyrin (1:4000, Synaptic Systems, 147 111), rabbit anti-GFP (1:1000; Invitrogen A-11122), rabbit anti-mGluR1 (1:500, Cell Signaling Technology, 12 551), rabbit antiMNK (1:100, Cell Signaling Technology, 2195), rabbit anti-p-MNK (1:20, Cell Signaling Technology, 2111), mouse anti-mTOR (1:1000, CST, 4517), rabbit anti-p-mTOR (1:50, CST, 5536), rabbit anti-PI3K (1:3000, Cell Signaling Technology, 4249), rabbit anti-p-PI3K (1:20, Cell Signaling Technology, 17 366), rabbit anti-PSD95 (1:100, Cell Signaling Technology, 3409), rabbit anti-Rps6 (1:100, Cell Signaling Technology, 2217), rabbit anti-S6K (1:200, CST, 33 475), rabbit anti-p-S6K (1:50, CST, 9234), mouse antisynapsin1 (1:7000, Synaptic Systems, 106 011), mouse anti-VGAT (1:20, Synaptic Systems, 131 011),mouse anti-vGlut1 (1:7000, Synaptic Systems, 135 011), and rabbit anti-vGlut2 (1:100, Cell Signaling Technology, 16 066). .. RNA Library Construction and Sequencing (Bulk RNA-seq): Total RNA of OBs was isolated using the RNeasy Lipid Tissue Mini Kit (Qiagen, Hilden, Germany).

Image Search Results

(a) Normalized relative mRNA levels of eft201 (eEF2, purple), tif51 (eIF5A, blue), oga1 (Stm1, green), and rtc3 (SNOR, red) at days 1 (diagonal stripes), 2 (checkered), and 3 (horizontal stripes) of glucose depletion (n = 3 biologically independent samples). Data are shown as mean ± s.d.. Statistical analysis was performed using one-way ANOVA. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. (b) Immunoblot analysis of SNOR levels in S. pombe cell lysates collected after 1, 4, and 7 days of glucose depletion. SNOR was detected using anti-FLAG antibody; GAPDH served as a loading control. (c) Immunoblot analysis of SNOR binding to 40S, 60S, and 80S ribosomal subunits using co-sedimentation assays. SNOR was detected via His-tag; Rps6 was used as a loading control. (d) Cryo-EM reconstruction of the in vitro reconstituted complex between the ribosomal large subunit and SNOR. Ribosomal proteins are shown in blue, rRNA in gray, and SNOR density in coral. (e) Close-up view of the atomic model showing SNOR bound to the peptidyl transferase center (PTC) of the ribosome. (f) Structural comparison of an AlphaFold model of SBDS/Sdo1 (left, green) and SNOR (right, coral) atomic models.

Journal: bioRxiv

Article Title: A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy

doi: 10.64898/2026.03.21.713407

Figure Lengend Snippet: (a) Normalized relative mRNA levels of eft201 (eEF2, purple), tif51 (eIF5A, blue), oga1 (Stm1, green), and rtc3 (SNOR, red) at days 1 (diagonal stripes), 2 (checkered), and 3 (horizontal stripes) of glucose depletion (n = 3 biologically independent samples). Data are shown as mean ± s.d.. Statistical analysis was performed using one-way ANOVA. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. (b) Immunoblot analysis of SNOR levels in S. pombe cell lysates collected after 1, 4, and 7 days of glucose depletion. SNOR was detected using anti-FLAG antibody; GAPDH served as a loading control. (c) Immunoblot analysis of SNOR binding to 40S, 60S, and 80S ribosomal subunits using co-sedimentation assays. SNOR was detected via His-tag; Rps6 was used as a loading control. (d) Cryo-EM reconstruction of the in vitro reconstituted complex between the ribosomal large subunit and SNOR. Ribosomal proteins are shown in blue, rRNA in gray, and SNOR density in coral. (e) Close-up view of the atomic model showing SNOR bound to the peptidyl transferase center (PTC) of the ribosome. (f) Structural comparison of an AlphaFold model of SBDS/Sdo1 (left, green) and SNOR (right, coral) atomic models.

Article Snippet: Primary antibodies used: 6xHis (Genscript, cat no. A00186), RPS6 (Cell Signaling, cat. no. 2217).

Techniques: Western Blot, Control, Binding Assay, Sedimentation, Cryo-EM Sample Prep, In Vitro, Comparison

(a) Slab view of the S. pombe hibernating ribosome atomic model shown as surface, highlighting insertion of the SNOR C-terminal tail into the polypeptide exit tunnel (PET, dashed line). Ribosomal RNA is shown in gray; small subunit proteins in yellow; large subunit proteins in blue; eEF2 in purple; Stm1 in green; SNOR in coral. (b) Structural comparison of SNOR and P-site tRNA binding site (PDB: 9AXV). Ribosomal protein and RNA are shown as a gray surface; SNOR is depicted as a coral cartoon; P-site tRNA is shown in orange. (c) Comparison of SNOR and SBDS tail (PDB: 6QKL) insertion into the PET. Atomic models of SNOR and SBDS are shown in coral and green, respectively. (d) Multiple sequence alignment of S. pombe SNOR with homologs from four fungal species (top) and with S. cerevisiae and human SBDS (bottom), highlighting conserved ribosome-contacting residues: E43 and E46 (lilac), K68 (purple), H96 and R97 (teal), and G100 (coral), which was selected for C-terminal truncation. Alignment generated using ESPript 3.0. (e) Close-up view of SNOR residue K68 (purple) contacting ribosomal RNA helix. (f) Close-up of SNOR residues E43 and E46 (lilac) contacting ribosomal protein uL16 (blue), and residues H96 and R97 (teal) contacting ribosomal RNA. PET location indicated by dashed red line. (g) Immunoblot analysis of ribosome co-sedimentation assay showing interaction of wildtype SNOR and SNOR mutants (G100STOP, K68E, H96A/R97E, K68E/H96A/R97E, and E43A/D46A) with purified S. pombe 80S ribosomes. SNOR was detected via His-tag; Rps6 served as a loading control.

Journal: bioRxiv

Article Title: A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy

doi: 10.64898/2026.03.21.713407

Figure Lengend Snippet: (a) Slab view of the S. pombe hibernating ribosome atomic model shown as surface, highlighting insertion of the SNOR C-terminal tail into the polypeptide exit tunnel (PET, dashed line). Ribosomal RNA is shown in gray; small subunit proteins in yellow; large subunit proteins in blue; eEF2 in purple; Stm1 in green; SNOR in coral. (b) Structural comparison of SNOR and P-site tRNA binding site (PDB: 9AXV). Ribosomal protein and RNA are shown as a gray surface; SNOR is depicted as a coral cartoon; P-site tRNA is shown in orange. (c) Comparison of SNOR and SBDS tail (PDB: 6QKL) insertion into the PET. Atomic models of SNOR and SBDS are shown in coral and green, respectively. (d) Multiple sequence alignment of S. pombe SNOR with homologs from four fungal species (top) and with S. cerevisiae and human SBDS (bottom), highlighting conserved ribosome-contacting residues: E43 and E46 (lilac), K68 (purple), H96 and R97 (teal), and G100 (coral), which was selected for C-terminal truncation. Alignment generated using ESPript 3.0. (e) Close-up view of SNOR residue K68 (purple) contacting ribosomal RNA helix. (f) Close-up of SNOR residues E43 and E46 (lilac) contacting ribosomal protein uL16 (blue), and residues H96 and R97 (teal) contacting ribosomal RNA. PET location indicated by dashed red line. (g) Immunoblot analysis of ribosome co-sedimentation assay showing interaction of wildtype SNOR and SNOR mutants (G100STOP, K68E, H96A/R97E, K68E/H96A/R97E, and E43A/D46A) with purified S. pombe 80S ribosomes. SNOR was detected via His-tag; Rps6 served as a loading control.

Article Snippet: Primary antibodies used: 6xHis (Genscript, cat no. A00186), RPS6 (Cell Signaling, cat. no. 2217).

Techniques: Comparison, Binding Assay, Sequencing, Generated, Residue, Western Blot, Sedimentation, Purification, Control

$(a) Atomic model of the S. pombe hibernating ribosome shown as a surface representation. Ribosomal RNA is depicted in gray; small subunit proteins in yellow; large subunit proteins in blue; eEF2 in purple; Stm1 in green; eIF5A in teal; SNOR in coral. (b) Close-up view of the SNOR–eIF5A–L1 tripartite interface locking the L1 stalk. SNOR is shown in coral; eIF5A in teal; ribosomal protein uL1 in navy; rRNA helices 68 and 69 in gray; the L1 stalk is highlighted in charcoal. (c) Conformational comparison of the L1 stalk in “open” (pink, PDB: 6WOO) versus “closed” (green) states. The ribosome atomic model is shown as cartoon; the cryo-ET map shown as a semi-transparent surface. (d-e) Close-up views of potential SNOR–eIF5A interaction interfaces involving SNOR residues S54/N55/N56 and E70/N73 (shown in red) and eIF5A (teal). (f) In vitro translation assay using rabbit reticulocyte lysate (RRL) comparing FLAG-tagged reporter levels in the presence of wildtype SNOR and mutants and/or eIF5A, compared to BSA control, assessed by immunoblot, done as independent duplicates. (g) Overlay of polysome gradient profiles from S. pombe cells grown in EMM with 0.5% glucose for 3 days under non-expressing (control, gray) and expressing (blue and pink) conditions, measured by absorbance at 260 nm (top). Distribution of SNOR, Rps6 and GAPDH across gradient fractions was assessed by immunoblotting (bottom).$

Journal: bioRxiv

Article Title: A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy

doi: 10.64898/2026.03.21.713407

Figure Lengend Snippet: (a) Atomic model of the S. pombe hibernating ribosome shown as a surface representation. Ribosomal RNA is depicted in gray; small subunit proteins in yellow; large subunit proteins in blue; eEF2 in purple; Stm1 in green; eIF5A in teal; SNOR in coral. (b) Close-up view of the SNOR–eIF5A–L1 tripartite interface locking the L1 stalk. SNOR is shown in coral; eIF5A in teal; ribosomal protein uL1 in navy; rRNA helices 68 and 69 in gray; the L1 stalk is highlighted in charcoal. (c) Conformational comparison of the L1 stalk in “open” (pink, PDB: 6WOO) versus “closed” (green) states. The ribosome atomic model is shown as cartoon; the cryo-ET map shown as a semi-transparent surface. (d-e) Close-up views of potential SNOR–eIF5A interaction interfaces involving SNOR residues S54/N55/N56 and E70/N73 (shown in red) and eIF5A (teal). (f) In vitro translation assay using rabbit reticulocyte lysate (RRL) comparing FLAG-tagged reporter levels in the presence of wildtype SNOR and mutants and/or eIF5A, compared to BSA control, assessed by immunoblot, done as independent duplicates. (g) Overlay of polysome gradient profiles from S. pombe cells grown in EMM with 0.5% glucose for 3 days under non-expressing (control, gray) and expressing (blue and pink) conditions, measured by absorbance at 260 nm (top). Distribution of SNOR, Rps6 and GAPDH across gradient fractions was assessed by immunoblotting (bottom).

Article Snippet: Primary antibodies used: 6xHis (Genscript, cat no. A00186), RPS6 (Cell Signaling, cat. no. 2217).

Techniques: Comparison, Tomography, In Vitro, Control, Western Blot, Expressing

A low concentration of dynasore (40 µM) activates phosphorylated-RPS6 and accumulation of SQSTM1 in growing metatarsal bones. A Bones treated with 40 µM of dynasore showed higher accumulations of SQSTM1 (white arrowheads in insets) and increased levels of phosphorylated-RPS6 (white arrows in insets) in the growth plate, as visualised by immunofluorescence. B, C Quantifications of SQSTM1 and phosphorylated-RPS6. Baf: bafilomycin. Each data point was obtained from an independent experiment containing 3 bones per group; data is presented as mean ± SD. *p < 0.05, **p < 0.01.

Journal: bioRxiv

Article Title: Dynasore, the dynamin inhibitor, modulates longitudinal bone growth in a hormetic manner

doi: 10.64898/2026.03.09.709778

Figure Lengend Snippet: A low concentration of dynasore (40 µM) activates phosphorylated-RPS6 and accumulation of SQSTM1 in growing metatarsal bones. A Bones treated with 40 µM of dynasore showed higher accumulations of SQSTM1 (white arrowheads in insets) and increased levels of phosphorylated-RPS6 (white arrows in insets) in the growth plate, as visualised by immunofluorescence. B, C Quantifications of SQSTM1 and phosphorylated-RPS6. Baf: bafilomycin. Each data point was obtained from an independent experiment containing 3 bones per group; data is presented as mean ± SD. *p < 0.05, **p < 0.01.

Article Snippet: Primary antibodies targeting phospho-RPS6 (1:100; Cell Signaling, catalog number: 4858) and SQSTM1 (1:500; Progen, catalog number: GP62-C) were diluted in the blocking buffer and incubated with the samples overnight at 4 °C.

Techniques: Concentration Assay, Immunofluorescence

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anti phospho rps6 antibody (Cell Signaling Technology Inc)

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