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Cell Signaling Technology Inc phospho immune complex
Phospho Immune Complex, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/phospho immune complex/product/Cell Signaling Technology Inc
Average 88 stars, based on 1 article reviews
Price from $9.99 to $1999.99
phospho immune complex - by Bioz Stars, 2020-07
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Article Title: Transcriptional and Post-translational Modifications of B-Raf in Quinol-Thioether Induced Tuberous Sclerosis Renal Cell Carcinoma
Article Snippet: .. Each phospho-immune complex (2-4 μg of B-Raf, Raf-1, A-Raf, and 14-3-3 isoforms; Cell Signaling Technologies, Danvers, MA) were added to microcentrifuge tubes containing 5 mg of QTRRE tissue lysates and protein-A/G sepharose beads (Amersham, Pittsburgh, PA), and incubated with rotation for 18 h at 4°C. .. Microcentrifuge tubes were centrifuged at 7500 g for 2 min at 4°C, supernatant was removed, and beads were washed three times with ice-cold cell lysis buffer.

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    Cell Signaling Technology Inc phospho akt t308
    AKT3 overexpression and siRNA knockdown affected expression of signaling proteins in PC-3 cells Protein expression of total <t>AKT,</t> AKT3, phospho-AKT S473, phospho-AKT <t>T308,</t> c-Myc, Skp2, p21 Cip , p27 Kip , cyclin D1, cyclin E, GSK3α, phospho-GSK-3α S21, GSK3β, phospho-GSK-3β S9, B-Raf, TSC1, TSC2, mTOR, phosphor-mTOR S2448, p70S6K, phopsho-p70S6K T421/S424 in PC-3 vector control, PC-3 overexpressing AKT3, PC-3 scramble control, and PC-3 AKT3 siRNA knockdown was assayed by Western blotting. Protein abundance of α-tubulin and β-actin were used as loading control.
    Phospho Akt T308, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho akt t308/product/Cell Signaling Technology Inc
    Average 99 stars, based on 30 article reviews
    Price from $9.99 to $1999.99
    phospho akt t308 - by Bioz Stars, 2020-07
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    99
    Cell Signaling Technology Inc anti phospho jnk
    Differential activation of SAPK isoforms during simulated ischaemia. Primary neonatal cardiac myocytes were subjected to simulated ischaemia for the times indicated and cell lysates examined by SDS–PAGE and western blotting with anti-phospho <t>p38</t> and anti-phospho <t>JNK</t> antibodies. As a positive control, cells were osmotically shocked (OS) by treatment with 0.5 M sorbitol for 20 min (A). The range of p38 isoforms expressed in unstimulated neonatal cardiac myocytes was determined by RT-PCR analysis using isoform-specific primers (B; top panel). cDNAs for p38α, β, γ and δ were used as positive controls (lower panel). Primary neonatal cardiac myocytes were transfected with Flag-tagged p38 isoforms α, β, γ and δ. The cells were subjected to simulated ischaemia for 20 min (C) or treated with 0.5 M sorbitol for 20 min (D). Transfected p38 was immunoprecipitated from the cell extracts using anti-Flag antibody and assayed in an immune-complex kinase assay.
    Anti Phospho Jnk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho jnk/product/Cell Signaling Technology Inc
    Average 99 stars, based on 74 article reviews
    Price from $9.99 to $1999.99
    anti phospho jnk - by Bioz Stars, 2020-07
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    Cell Signaling Technology Inc phospho mtor
    Maternal uncoupling protein-1 (UCP1) deficiency increased fetal growth and placental efficiency. Fetuses and placentas were collected from Ucp1 −/− and wild-type (WT) cross-mated dams at embryonic day (E)18.5 through C-section. Significantly increased fetal weight ( A ) and crown-rump length ( B ) were detected in fetuses of Ucp1 −/− dams (FUKOD). Fetal blood glucose concentrations ( C ), but not triglycerides (TG) and free fatty acids (FFA) (pooled sample per litter, D and E ), were remarkably elevated in FUKOD vs. fetuses from WT dams (FWTD). Despite no difference in placental weight ( F ), fetal/placental weight ratios were significantly increased in FUKOD ( G ). Expression levels of key nutrient transporters and signal pathways were measured by Western blotting and real-PCR using samples from placentas at E18.5 ( H and I ). <t>p-Akt,</t> phospho-protein kinase B; <t>p-mTOR,</t> phospho-mammalian target of rapamycin; p-AMPK, phospho-AMP-avtivated protein kinase. Data are presented as means ± SE. Per litter averages of body weight, length, glucose, placental weight, and fetal/placental weight ratio were used for statistical analysis; n = 7–9 for A–G , n = 12 for h H and I . * P
    Phospho Mtor, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 366 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho mtor/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc phospho s6
    Angiomyolipomas. Gross pictures, micrographs of H E stains, and immunohistochemical stains with <t>anti-phospho-S6</t> (S235/S236, P-S6) of AML200, AML227 and AML234 are shown. AML227 arose in the lower pole of the kidney and extended to the attached colon (arrow). AML234 arose adjacent to the kidney. A small renal cell carcinoma is present in the kidney parenchyma (arrowhead).
    Phospho S6, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 244 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho s6/product/Cell Signaling Technology Inc
    Average 99 stars, based on 244 article reviews
    Price from $9.99 to $1999.99
    phospho s6 - by Bioz Stars, 2020-07
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    AKT3 overexpression and siRNA knockdown affected expression of signaling proteins in PC-3 cells Protein expression of total AKT, AKT3, phospho-AKT S473, phospho-AKT T308, c-Myc, Skp2, p21 Cip , p27 Kip , cyclin D1, cyclin E, GSK3α, phospho-GSK-3α S21, GSK3β, phospho-GSK-3β S9, B-Raf, TSC1, TSC2, mTOR, phosphor-mTOR S2448, p70S6K, phopsho-p70S6K T421/S424 in PC-3 vector control, PC-3 overexpressing AKT3, PC-3 scramble control, and PC-3 AKT3 siRNA knockdown was assayed by Western blotting. Protein abundance of α-tubulin and β-actin were used as loading control.

    Journal: Oncotarget

    Article Title: AKT3 promotes prostate cancer proliferation cells through regulation of Akt, B-Raf TSC1/TSC2

    doi:

    Figure Lengend Snippet: AKT3 overexpression and siRNA knockdown affected expression of signaling proteins in PC-3 cells Protein expression of total AKT, AKT3, phospho-AKT S473, phospho-AKT T308, c-Myc, Skp2, p21 Cip , p27 Kip , cyclin D1, cyclin E, GSK3α, phospho-GSK-3α S21, GSK3β, phospho-GSK-3β S9, B-Raf, TSC1, TSC2, mTOR, phosphor-mTOR S2448, p70S6K, phopsho-p70S6K T421/S424 in PC-3 vector control, PC-3 overexpressing AKT3, PC-3 scramble control, and PC-3 AKT3 siRNA knockdown was assayed by Western blotting. Protein abundance of α-tubulin and β-actin were used as loading control.

    Article Snippet: Protein expression was determined by Western blotting using following antibodies: phospho-AKT S473, phospho-AKT T308, β-catenin, GSK3α, GSK3β, phospho-GSK-3α S21, phospho-GSK-3β S9, cyclin D1, cyclin E, mTOR, and total AKT antibodies were from Cell Signaling (Danvers, MA, U.S.A.); c-Myc, TSC1, TSC2, B-Raf, and phospho-p70S6K T421/S424 antibodies were from Epitomics (Burlingame, CA, U.S.A.); p21Cip1 , p27Kip1 , and Skp2 antibodies were from Santa Cruz (Santa Cruz, CA, U.S.A.); AKT3, phospho-mTOR S2448 and p70S6K antibodies were purchased from Millipore (Billerica, MA, U.S.A.); β-actin antibody was from Novus (Littleton, CO, U.S.A.);α-tubulin antibody was from Sigma (St. Louis, MO, U.S.A.).

    Techniques: Over Expression, Expressing, Plasmid Preparation, Western Blot

    Differential activation of SAPK isoforms during simulated ischaemia. Primary neonatal cardiac myocytes were subjected to simulated ischaemia for the times indicated and cell lysates examined by SDS–PAGE and western blotting with anti-phospho p38 and anti-phospho JNK antibodies. As a positive control, cells were osmotically shocked (OS) by treatment with 0.5 M sorbitol for 20 min (A). The range of p38 isoforms expressed in unstimulated neonatal cardiac myocytes was determined by RT-PCR analysis using isoform-specific primers (B; top panel). cDNAs for p38α, β, γ and δ were used as positive controls (lower panel). Primary neonatal cardiac myocytes were transfected with Flag-tagged p38 isoforms α, β, γ and δ. The cells were subjected to simulated ischaemia for 20 min (C) or treated with 0.5 M sorbitol for 20 min (D). Transfected p38 was immunoprecipitated from the cell extracts using anti-Flag antibody and assayed in an immune-complex kinase assay.

    Journal: Biochimica et Biophysica Acta

    Article Title: Activation of ASK1, downstream MAPKK and MAPK isoforms during cardiac ischaemia

    doi: 10.1016/j.bbadis.2010.06.005

    Figure Lengend Snippet: Differential activation of SAPK isoforms during simulated ischaemia. Primary neonatal cardiac myocytes were subjected to simulated ischaemia for the times indicated and cell lysates examined by SDS–PAGE and western blotting with anti-phospho p38 and anti-phospho JNK antibodies. As a positive control, cells were osmotically shocked (OS) by treatment with 0.5 M sorbitol for 20 min (A). The range of p38 isoforms expressed in unstimulated neonatal cardiac myocytes was determined by RT-PCR analysis using isoform-specific primers (B; top panel). cDNAs for p38α, β, γ and δ were used as positive controls (lower panel). Primary neonatal cardiac myocytes were transfected with Flag-tagged p38 isoforms α, β, γ and δ. The cells were subjected to simulated ischaemia for 20 min (C) or treated with 0.5 M sorbitol for 20 min (D). Transfected p38 was immunoprecipitated from the cell extracts using anti-Flag antibody and assayed in an immune-complex kinase assay.

    Article Snippet: The phosphorylation site-specific antibodies anti-phospho-p38 (Cat. no. 9211), anti-phospho-JNK (Cat. no. 9251) and anti-phospho-Thr 845 ASK1 (Cat. no. 3765) were from Cell Signalling Technology.

    Techniques: Activation Assay, SDS Page, Western Blot, Positive Control, Reverse Transcription Polymerase Chain Reaction, Transfection, Immunoprecipitation, Immune Complex Kinase Assay

    Differential activation of SAPK activators during cardiac ischaemia in perfused hearts. Freshly isolated perfused rat hearts were subjected to global ischaemia for the times indicated, extracted and assayed for MKK3 (A), MKK6 (B), MKK4 (C) and MKK7 (D) activity by coupled immune-complex kinase assay. Extracts prepared from hearts perfused without (Con) or with 0.5 M sorbitol were used in control MKK assays lacking either GST-p38/JNK (no MAPK), GST-ATF2/Jun (no substrate) or immunoprecipitated with control antiserum (E). Extracts of HEK 293 cells, transfected with Flag-tagged MKKs, were immunoprecipitated with either control serum or antisera specific for the various MKKs assayed. Immunoprecipitated MKKs were detected by western blotting with anti-Flag antibody (F).

    Journal: Biochimica et Biophysica Acta

    Article Title: Activation of ASK1, downstream MAPKK and MAPK isoforms during cardiac ischaemia

    doi: 10.1016/j.bbadis.2010.06.005

    Figure Lengend Snippet: Differential activation of SAPK activators during cardiac ischaemia in perfused hearts. Freshly isolated perfused rat hearts were subjected to global ischaemia for the times indicated, extracted and assayed for MKK3 (A), MKK6 (B), MKK4 (C) and MKK7 (D) activity by coupled immune-complex kinase assay. Extracts prepared from hearts perfused without (Con) or with 0.5 M sorbitol were used in control MKK assays lacking either GST-p38/JNK (no MAPK), GST-ATF2/Jun (no substrate) or immunoprecipitated with control antiserum (E). Extracts of HEK 293 cells, transfected with Flag-tagged MKKs, were immunoprecipitated with either control serum or antisera specific for the various MKKs assayed. Immunoprecipitated MKKs were detected by western blotting with anti-Flag antibody (F).

    Article Snippet: The phosphorylation site-specific antibodies anti-phospho-p38 (Cat. no. 9211), anti-phospho-JNK (Cat. no. 9251) and anti-phospho-Thr 845 ASK1 (Cat. no. 3765) were from Cell Signalling Technology.

    Techniques: Activation Assay, Isolation, Activity Assay, Immune Complex Kinase Assay, Immunoprecipitation, Transfection, Western Blot

    Time course of SAPK activation during cardiac ischaemia. Freshly isolated perfused rat hearts were subjected to global ischaemia for the times indicated, extracted and assayed for p38 (A) or JNK (B) activity by immune-complex kinase assay. The range of p38 isoforms expressed in the normal adult rat heart was determined by RT-PCR analysis with isoform-specific primers using tissue from unstimulated hearts (C; upper panel). cDNAs for p38α, β, γ and δ were used as positive controls (lower panel). The isoform specificity of the p38 antibody used in immune-complex kinase assays was determined by immunoprecipitation from cell lysates containing epitope-tagged forms of p38α, β, γ and δ, followed by SDS–PAGE and western blotting with anti-Flag antibody (D).

    Journal: Biochimica et Biophysica Acta

    Article Title: Activation of ASK1, downstream MAPKK and MAPK isoforms during cardiac ischaemia

    doi: 10.1016/j.bbadis.2010.06.005

    Figure Lengend Snippet: Time course of SAPK activation during cardiac ischaemia. Freshly isolated perfused rat hearts were subjected to global ischaemia for the times indicated, extracted and assayed for p38 (A) or JNK (B) activity by immune-complex kinase assay. The range of p38 isoforms expressed in the normal adult rat heart was determined by RT-PCR analysis with isoform-specific primers using tissue from unstimulated hearts (C; upper panel). cDNAs for p38α, β, γ and δ were used as positive controls (lower panel). The isoform specificity of the p38 antibody used in immune-complex kinase assays was determined by immunoprecipitation from cell lysates containing epitope-tagged forms of p38α, β, γ and δ, followed by SDS–PAGE and western blotting with anti-Flag antibody (D).

    Article Snippet: The phosphorylation site-specific antibodies anti-phospho-p38 (Cat. no. 9211), anti-phospho-JNK (Cat. no. 9251) and anti-phospho-Thr 845 ASK1 (Cat. no. 3765) were from Cell Signalling Technology.

    Techniques: Activation Assay, Isolation, Activity Assay, Immune Complex Kinase Assay, Reverse Transcription Polymerase Chain Reaction, Immunoprecipitation, SDS Page, Western Blot

    Maternal uncoupling protein-1 (UCP1) deficiency increased fetal growth and placental efficiency. Fetuses and placentas were collected from Ucp1 −/− and wild-type (WT) cross-mated dams at embryonic day (E)18.5 through C-section. Significantly increased fetal weight ( A ) and crown-rump length ( B ) were detected in fetuses of Ucp1 −/− dams (FUKOD). Fetal blood glucose concentrations ( C ), but not triglycerides (TG) and free fatty acids (FFA) (pooled sample per litter, D and E ), were remarkably elevated in FUKOD vs. fetuses from WT dams (FWTD). Despite no difference in placental weight ( F ), fetal/placental weight ratios were significantly increased in FUKOD ( G ). Expression levels of key nutrient transporters and signal pathways were measured by Western blotting and real-PCR using samples from placentas at E18.5 ( H and I ). p-Akt, phospho-protein kinase B; p-mTOR, phospho-mammalian target of rapamycin; p-AMPK, phospho-AMP-avtivated protein kinase. Data are presented as means ± SE. Per litter averages of body weight, length, glucose, placental weight, and fetal/placental weight ratio were used for statistical analysis; n = 7–9 for A–G , n = 12 for h H and I . * P

    Journal: American Journal of Physiology - Endocrinology and Metabolism

    Article Title: Browning and Beiging of Adipose Tissue: Its Role in the Regulation of Energy Homeostasis and as a Potential Target for Alleviating Metabolic Diseases: Regulatory effects of brown adipose tissue thermogenesis on maternal metabolic adaptation, placental efficiency, and fetal growth in mice

    doi: 10.1152/ajpendo.00192.2018

    Figure Lengend Snippet: Maternal uncoupling protein-1 (UCP1) deficiency increased fetal growth and placental efficiency. Fetuses and placentas were collected from Ucp1 −/− and wild-type (WT) cross-mated dams at embryonic day (E)18.5 through C-section. Significantly increased fetal weight ( A ) and crown-rump length ( B ) were detected in fetuses of Ucp1 −/− dams (FUKOD). Fetal blood glucose concentrations ( C ), but not triglycerides (TG) and free fatty acids (FFA) (pooled sample per litter, D and E ), were remarkably elevated in FUKOD vs. fetuses from WT dams (FWTD). Despite no difference in placental weight ( F ), fetal/placental weight ratios were significantly increased in FUKOD ( G ). Expression levels of key nutrient transporters and signal pathways were measured by Western blotting and real-PCR using samples from placentas at E18.5 ( H and I ). p-Akt, phospho-protein kinase B; p-mTOR, phospho-mammalian target of rapamycin; p-AMPK, phospho-AMP-avtivated protein kinase. Data are presented as means ± SE. Per litter averages of body weight, length, glucose, placental weight, and fetal/placental weight ratio were used for statistical analysis; n = 7–9 for A–G , n = 12 for h H and I . * P

    Article Snippet: Antibodies against phospho-Akt (Ser473 ), phospho-mTOR (mammalian target of rapamycin), phospho-AMP-activated protein kinase (AMPK, Thr172 ), Akt, mTOR, and AMPK were from Cell Signaling (Danvers, MA).

    Techniques: Expressing, Western Blot, Polymerase Chain Reaction

    Angiomyolipomas. Gross pictures, micrographs of H E stains, and immunohistochemical stains with anti-phospho-S6 (S235/S236, P-S6) of AML200, AML227 and AML234 are shown. AML227 arose in the lower pole of the kidney and extended to the attached colon (arrow). AML234 arose adjacent to the kidney. A small renal cell carcinoma is present in the kidney parenchyma (arrowhead).

    Journal: PLoS ONE

    Article Title: Angiomyolipoma Have Common Mutations in TSC2 but No Other Common Genetic Events

    doi: 10.1371/journal.pone.0024919

    Figure Lengend Snippet: Angiomyolipomas. Gross pictures, micrographs of H E stains, and immunohistochemical stains with anti-phospho-S6 (S235/S236, P-S6) of AML200, AML227 and AML234 are shown. AML227 arose in the lower pole of the kidney and extended to the attached colon (arrow). AML234 arose adjacent to the kidney. A small renal cell carcinoma is present in the kidney parenchyma (arrowhead).

    Article Snippet: Antibodies to phospho-S6 (Ser235/236;Cell Signaling Technology #2211; 1∶200 dilution) or Clone HMB-45 (Dako IR052, 1∶50 dilution) diluted in 5% normal goat in TBST with Biotin were applied and incubated overnight at 4°C.

    Techniques: Immunohistochemistry