sirna sequences (Santa Cruz Biotechnology)

Santa Cruz Biotechnology is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Santa Cruz Biotechnology sirna sequences

Figure 1 EGFR inhibition triggers an adaptive response in glioma cells. (a) Western blot showing EGFR levels in established GBM cell lines and patient- derived primary GBM neurospheres. U87 vector indicates U87MG cells transfected with an empty vector. U251 is an established GBM cell line. β-actin was used as a loading control. (b) Patient-derived primary GBM neurospheres (GBM9) were exposed to erlotinib (1 µM) for the indicated times followed by western blot with the indicated antibodies; pMet, pAxl, pERK, pEGFR, pSTAT3 and pAkt specifically detect phosphorylated isoforms. (c,d) A similar experiment in GBM neurospheres derived from two different patients (GBM39 and SK987). (e) U87EGFR cells were treated with erlotinib (1 µM) for the indicated times followed by western blot with the indicated antibodies. (f) A similar experiment was conducted in U87EGFRvIII cells. <t>(g–j)</t> <t>Axl</t> was inhibited using the specific inhibitor R428 (1 µM). Cells were exposed to erlotinib followed by western blot. Erlotinib-induced ERK activation is inhibited when the Axl inhibitor is used in both established GBM cell lines and patient-derived neurospheres. (k–n) <t>siRNA</t> knockdown of Axl results in an inhibition of erlotinib-induced ERK activation in both established cell lines and patient-derived neurospheres. Control siRNA or Axl siRNA was transfected into cells (for 48 h), followed by addition of erlotinib for 48 h and western blot with indicated antibodies. Western blots shown in a–n are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 11.

Sirna Sequences, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 501 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/small+pool+pcr+techniques/TNF-R1/pm28604685-643-8-22
Average 94 stars, based on 501 article reviews

sirna sequences - by Bioz Stars, 2026-09

94/100 stars

Images

1) Product Images from "A TNF-JNK-Axl-ERK signaling axis mediates primary resistance to EGFR inhibition in glioblastoma."

Article Title: A TNF-JNK-Axl-ERK signaling axis mediates primary resistance to EGFR inhibition in glioblastoma.

Journal: Nature neuroscience

doi: 10.1038/nn.4584

Figure Legend Snippet: Figure 1 EGFR inhibition triggers an adaptive response in glioma cells. (a) Western blot showing EGFR levels in established GBM cell lines and patient- derived primary GBM neurospheres. U87 vector indicates U87MG cells transfected with an empty vector. U251 is an established GBM cell line. β-actin was used as a loading control. (b) Patient-derived primary GBM neurospheres (GBM9) were exposed to erlotinib (1 µM) for the indicated times followed by western blot with the indicated antibodies; pMet, pAxl, pERK, pEGFR, pSTAT3 and pAkt specifically detect phosphorylated isoforms. (c,d) A similar experiment in GBM neurospheres derived from two different patients (GBM39 and SK987). (e) U87EGFR cells were treated with erlotinib (1 µM) for the indicated times followed by western blot with the indicated antibodies. (f) A similar experiment was conducted in U87EGFRvIII cells. (g–j) Axl was inhibited using the specific inhibitor R428 (1 µM). Cells were exposed to erlotinib followed by western blot. Erlotinib-induced ERK activation is inhibited when the Axl inhibitor is used in both established GBM cell lines and patient-derived neurospheres. (k–n) siRNA knockdown of Axl results in an inhibition of erlotinib-induced ERK activation in both established cell lines and patient-derived neurospheres. Control siRNA or Axl siRNA was transfected into cells (for 48 h), followed by addition of erlotinib for 48 h and western blot with indicated antibodies. Western blots shown in a–n are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 11.

Techniques Used: Inhibition, Western Blot, Derivative Assay, Plasmid Preparation, Transfection, Control, Activation Assay, Knockdown

Figure 2 EGFR inhibition–induced Axl and ERK activation is mediated by JNK. (a,b) Patient-derived primary GBM neurospheres were exposed to erlotinib for 48 h in the presence or absence of the JNK inhibitor SP600125 (1 µM) or p38 inhibitor SB203580 (10 µM), followed by western blot with the indicated antibodies. DMSO indicates vehicle alone. (c,d) U87EGFRwt or U87EGFRvIII cells were exposed to erlotinib for 48 h in the presence or absence of SP600125 or SB203580, followed by western blot with the indicated antibodies. (e,f) siRNA knockdown for JNK1 and JNK2 (siJNK) was conducted in GBM9 and GBM39 neurospheres, followed by exposure to erlotinib for 48 h and western blot with the indicated antibodies. siCtrl indicates scrambled control siRNA. (g) A similar experiment was done in U87EGFRwt cells. (h–k) JNK is activated in response to erlotinib in patient- derived primary neurospheres, as well as in established GBM cell lines, as determined by the phosphorylation of JNK. Western blots shown in a–k are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 12. (l) A luciferase reporter assay shows that EGFR inhibition with erlotinib results in an increase in AP-1 transcriptional activity in GBM9 and U87EGFRwt cells. Erlotinib was used for 24 h (1 µM). DMSO was used as a control (Ctrl). GBM9: Ctrl versus erlotinib: P = 0.0056, t = 5.43, d.f. = 4, **P < 0.01; U87EGFRwt: Ctrl versus erlotinib: P = 0.0061, t = 5.31, d.f. = 4, **P < 0.01. Data are presented as mean ± s.e.m. Significant difference analyzed by an unpaired Student’s t-test (n = 3 biologically independent experimental replicates).

Figure Legend Snippet: Figure 2 EGFR inhibition–induced Axl and ERK activation is mediated by JNK. (a,b) Patient-derived primary GBM neurospheres were exposed to erlotinib for 48 h in the presence or absence of the JNK inhibitor SP600125 (1 µM) or p38 inhibitor SB203580 (10 µM), followed by western blot with the indicated antibodies. DMSO indicates vehicle alone. (c,d) U87EGFRwt or U87EGFRvIII cells were exposed to erlotinib for 48 h in the presence or absence of SP600125 or SB203580, followed by western blot with the indicated antibodies. (e,f) siRNA knockdown for JNK1 and JNK2 (siJNK) was conducted in GBM9 and GBM39 neurospheres, followed by exposure to erlotinib for 48 h and western blot with the indicated antibodies. siCtrl indicates scrambled control siRNA. (g) A similar experiment was done in U87EGFRwt cells. (h–k) JNK is activated in response to erlotinib in patient- derived primary neurospheres, as well as in established GBM cell lines, as determined by the phosphorylation of JNK. Western blots shown in a–k are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 12. (l) A luciferase reporter assay shows that EGFR inhibition with erlotinib results in an increase in AP-1 transcriptional activity in GBM9 and U87EGFRwt cells. Erlotinib was used for 24 h (1 µM). DMSO was used as a control (Ctrl). GBM9: Ctrl versus erlotinib: P = 0.0056, t = 5.43, d.f. = 4, **P < 0.01; U87EGFRwt: Ctrl versus erlotinib: P = 0.0061, t = 5.31, d.f. = 4, **P < 0.01. Data are presented as mean ± s.e.m. Significant difference analyzed by an unpaired Student’s t-test (n = 3 biologically independent experimental replicates).

Techniques Used: Inhibition, Activation Assay, Derivative Assay, Western Blot, Knockdown, Control, Phospho-proteomics, Luciferase, Reporter Assay, Activity Assay

Figure 4 EGFR inhibition leads to increased TNF signaling that triggers an adaptive signaling pathway. (a,b) EGFR inhibition leads to an increase in TNF mRNA in patient-derived GBM9 and GBM39 neurospheres. Cells were exposed to erlotinib (100 nM) for the times indicated followed by real-time quantitative PCR for TNF mRNA. (a) 0 versus 24 h: P = 0.0019, t = 7.22, d.f. = 4. (b) 0 versus 4 h: P = 0.0102, t = 4.58, d.f. = 4; 0 versus 24 h: P = 0.0021, t = 7.10, d.f. = 4. (c,d) A similar experiment was conducted in U87EGFRwt and U87EGFRvIII cells using an erlotinib concentration of 1 µM. (c) 0 versus 4 h: P = 0.0018, t = 7.41, d.f. = 4; 0 versus 24 h: P = 0.0012, t = 8.20, d.f. = 4. (d) 0 versus 4 h: P = 0.0030, t = 6.46, d.f. = 4; 0 versus 24 h: P = 0.0054, t = 5.47, d.f. = 4. (e) A TNF ELISA was performed on supernatants from erlotinib treated U87EGFRwt and U87EGFRvIII cells (1 µM) and GBM9 and GBM39 neurospheres (100 nM). U87EGFRwt: 0 versus 24 h: P = 0.0056, t = 5.42, d.f. = 4; 0 versus 48 h: P = 0.0006, t = 10.4, d.f. = 4; U87EGFRVIII: 0 versus 24 h: P = 0.0022, t = 6.98, d.f. = 4; 0 versus 48 h: P = 0.0083, t = 4.86, d.f. = 4; GBM9: 0 versus 24 h: P = 0.01, t = 4.6, d.f. = 4; 0 versus 48 h: P = 0.0043, t = 5.84, d.f. = 4; GBM39: 0 versus 24 h: P = 0.0189, t = 3.82, d.f. = 4; 0 versus 48 h: P = 0.0024, t = 6.81, d.f. = 4. Data are presented as mean ± s.e.m.; *P < 0.05, **P < 0.01, ***P < 0.001 from two-tailed unpaired Student’s t-test (n = 3 biologically independent experimental replicates). (f) Time course of TNF upregulation in mouse tumors exposed to erlotinib 50 mg/kg for the indicated time points after formation of subcutaneous tumors (n = 3). Tumors were removed after erlotinib exposure, followed by TNF ELISA on protein extracts. 0 versus 1 d: P = 0.0045, t = 5.77, d.f. = 4; 0 versus 2 d: P = 0.0002, t = 13.92, d.f. = 4; 0 versus 7 d: P = 0.0245, t = 3.52, d.f. = 4. Data are presented as mean ± s.e.m.; *P < 0.05, **P < 0.01, ***P < 0.001 from a two-tailed unpaired Student’s t-test. (g) Signal transduction in tumors exposed to erlotinib (50 mg/kg) for the indicated time points. (h) A neutralizing antibody to TNF (TNF Ab) (2 µg/ml) blocked erlotinib-induced activation of Axl, ERK and JNK in GBM9 and GBM39 neurospheres and U87EGFRwt and U87EGFRvIII cell lines, while control antibody (Ctrl Ab) had no effect. The control antibody was normal mouse IgG. (i) siRNA knockdown of TNFR1 (siTNFR1) blocked erlotinib-induced activation of Axl, ERK and JNK in GBM9 and GBM39 neurospheres and in U87EGFRwt and U87EGFRvIII cell lines, while control (scrambled) siRNA (siCtrl) had no effect. Western blots shown in g–i are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 13.

Figure Legend Snippet: Figure 4 EGFR inhibition leads to increased TNF signaling that triggers an adaptive signaling pathway. (a,b) EGFR inhibition leads to an increase in TNF mRNA in patient-derived GBM9 and GBM39 neurospheres. Cells were exposed to erlotinib (100 nM) for the times indicated followed by real-time quantitative PCR for TNF mRNA. (a) 0 versus 24 h: P = 0.0019, t = 7.22, d.f. = 4. (b) 0 versus 4 h: P = 0.0102, t = 4.58, d.f. = 4; 0 versus 24 h: P = 0.0021, t = 7.10, d.f. = 4. (c,d) A similar experiment was conducted in U87EGFRwt and U87EGFRvIII cells using an erlotinib concentration of 1 µM. (c) 0 versus 4 h: P = 0.0018, t = 7.41, d.f. = 4; 0 versus 24 h: P = 0.0012, t = 8.20, d.f. = 4. (d) 0 versus 4 h: P = 0.0030, t = 6.46, d.f. = 4; 0 versus 24 h: P = 0.0054, t = 5.47, d.f. = 4. (e) A TNF ELISA was performed on supernatants from erlotinib treated U87EGFRwt and U87EGFRvIII cells (1 µM) and GBM9 and GBM39 neurospheres (100 nM). U87EGFRwt: 0 versus 24 h: P = 0.0056, t = 5.42, d.f. = 4; 0 versus 48 h: P = 0.0006, t = 10.4, d.f. = 4; U87EGFRVIII: 0 versus 24 h: P = 0.0022, t = 6.98, d.f. = 4; 0 versus 48 h: P = 0.0083, t = 4.86, d.f. = 4; GBM9: 0 versus 24 h: P = 0.01, t = 4.6, d.f. = 4; 0 versus 48 h: P = 0.0043, t = 5.84, d.f. = 4; GBM39: 0 versus 24 h: P = 0.0189, t = 3.82, d.f. = 4; 0 versus 48 h: P = 0.0024, t = 6.81, d.f. = 4. Data are presented as mean ± s.e.m.; *P < 0.05, **P < 0.01, ***P < 0.001 from two-tailed unpaired Student’s t-test (n = 3 biologically independent experimental replicates). (f) Time course of TNF upregulation in mouse tumors exposed to erlotinib 50 mg/kg for the indicated time points after formation of subcutaneous tumors (n = 3). Tumors were removed after erlotinib exposure, followed by TNF ELISA on protein extracts. 0 versus 1 d: P = 0.0045, t = 5.77, d.f. = 4; 0 versus 2 d: P = 0.0002, t = 13.92, d.f. = 4; 0 versus 7 d: P = 0.0245, t = 3.52, d.f. = 4. Data are presented as mean ± s.e.m.; *P < 0.05, **P < 0.01, ***P < 0.001 from a two-tailed unpaired Student’s t-test. (g) Signal transduction in tumors exposed to erlotinib (50 mg/kg) for the indicated time points. (h) A neutralizing antibody to TNF (TNF Ab) (2 µg/ml) blocked erlotinib-induced activation of Axl, ERK and JNK in GBM9 and GBM39 neurospheres and U87EGFRwt and U87EGFRvIII cell lines, while control antibody (Ctrl Ab) had no effect. The control antibody was normal mouse IgG. (i) siRNA knockdown of TNFR1 (siTNFR1) blocked erlotinib-induced activation of Axl, ERK and JNK in GBM9 and GBM39 neurospheres and in U87EGFRwt and U87EGFRvIII cell lines, while control (scrambled) siRNA (siCtrl) had no effect. Western blots shown in g–i are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 13.

Techniques Used: Inhibition, Derivative Assay, Real-time Polymerase Chain Reaction, Concentration Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test, Transduction, Activation Assay, Control, Knockdown, Western Blot

Figure 6 TNF inhibition sensitizes glioma cells to EGFR inhibition. (a,b) AlamarBlue cell viability assay in GBM9 or GBM39 neurospheres. Etanercept (100 nM) sensitizes cells to EGFR inhibition with erlotinib. Etanercept and erlotinib were added to GBM9 or GBM39 neurospheres concurrently and AlamarBlue assay was done after 72 h. DMSO was used as a control. (a) Erlotinib versus erlotinib + etanercept: P = 0.0027, t = 6.59, d.f. = 4. (b) Erlotinib versus erlotinib + etanercept: P = 0.0044, t = 6.59, d.f. = 4. (c) A similar experiment was performed in U87EGFRwt cells. Erlotinib versus erlotinib + etanercept: P = 0.0056, t = 5.41, d.f. = 4. (d,e) TNFR1 was silenced using siRNA (siTNFR1) in GBM9 and GBM39 cells and cells were exposed to erlotinib for 72 h in stem cell medium without EGF for 72 h, followed by AlamarBlue assay. (d) Erlotinib + scrambled control siRNA (siCtrl) versus erlotinib + siTNFR1: P = 0.0014, t = 7.95, d.f. = 4. (e) Erlotinib + siCtrl versus erlotinib + siTNFR1: P = 0.0041, t = 5.90, d.f. = 4. (f) A similar experiment was done in U87EGFRwt cells. Erlotinib + siCtrl versus erlotinib + siTNFR1: P = 0.0021, t = 7.11, d.f. = 4. (g–i) Thalidomide sensitizes GBM9 and GBM39 cells to EGFR inhibition with erlotinib. Thalidomide (1 µM) and erlotinib were added to GBM9 and GBM39 neurospheres (100 nM) or U87EGFRwt cells (1 µM) concurrently and AlamarBlue assay was done after 72 h. (g) Erlotinib versus erlotinib + thalidomide: P = 0.0030, t = 6.42, d.f. = 4. (h) Erlotinib versus erlotinib + thalidomide: P = 0.0027, t = 6.59, d.f. = 4. (i) Erlotinib versus erlotinib + thalidomide: P = 0.0013, t = 8.11, d.f. = 4. (j,k) Etanercept or thalidomide blocks erlotinib-induced activation of JNK, Axl and ERK in GBM9 and GBM39 neurospheres, as shown by western blot. Control antibody (Ctrl Ab) is normal mouse IgG. (l) A similar experiment was conducted in U87EGFRwt cells. Western blots shown in j–l are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 14. (m,n) Exogenous TNF protects GBM9 and GBM39 neurospheres from erlotinib-induced cell death. TNF (1 ng/ml) and erlotinib (1 µM) were added to cells concurrently and AlamarBlue cell viability assay was done after 72 h. (m) Erlotinib versus erlotinib + TNF: P = 0.0018, t = 7.41, d.f. = 4. (n) Erlotinib versus erlotinib + TNF: P = 0.0087, t = 4.79, d.f. = 4. Data are presented as mean ± s.e.m.; **P < 0.01, ***P < 0.001 from two-tailed unpaired Student’s t-test (n = 3 biologically independent experimental replicates).

Figure Legend Snippet: Figure 6 TNF inhibition sensitizes glioma cells to EGFR inhibition. (a,b) AlamarBlue cell viability assay in GBM9 or GBM39 neurospheres. Etanercept (100 nM) sensitizes cells to EGFR inhibition with erlotinib. Etanercept and erlotinib were added to GBM9 or GBM39 neurospheres concurrently and AlamarBlue assay was done after 72 h. DMSO was used as a control. (a) Erlotinib versus erlotinib + etanercept: P = 0.0027, t = 6.59, d.f. = 4. (b) Erlotinib versus erlotinib + etanercept: P = 0.0044, t = 6.59, d.f. = 4. (c) A similar experiment was performed in U87EGFRwt cells. Erlotinib versus erlotinib + etanercept: P = 0.0056, t = 5.41, d.f. = 4. (d,e) TNFR1 was silenced using siRNA (siTNFR1) in GBM9 and GBM39 cells and cells were exposed to erlotinib for 72 h in stem cell medium without EGF for 72 h, followed by AlamarBlue assay. (d) Erlotinib + scrambled control siRNA (siCtrl) versus erlotinib + siTNFR1: P = 0.0014, t = 7.95, d.f. = 4. (e) Erlotinib + siCtrl versus erlotinib + siTNFR1: P = 0.0041, t = 5.90, d.f. = 4. (f) A similar experiment was done in U87EGFRwt cells. Erlotinib + siCtrl versus erlotinib + siTNFR1: P = 0.0021, t = 7.11, d.f. = 4. (g–i) Thalidomide sensitizes GBM9 and GBM39 cells to EGFR inhibition with erlotinib. Thalidomide (1 µM) and erlotinib were added to GBM9 and GBM39 neurospheres (100 nM) or U87EGFRwt cells (1 µM) concurrently and AlamarBlue assay was done after 72 h. (g) Erlotinib versus erlotinib + thalidomide: P = 0.0030, t = 6.42, d.f. = 4. (h) Erlotinib versus erlotinib + thalidomide: P = 0.0027, t = 6.59, d.f. = 4. (i) Erlotinib versus erlotinib + thalidomide: P = 0.0013, t = 8.11, d.f. = 4. (j,k) Etanercept or thalidomide blocks erlotinib-induced activation of JNK, Axl and ERK in GBM9 and GBM39 neurospheres, as shown by western blot. Control antibody (Ctrl Ab) is normal mouse IgG. (l) A similar experiment was conducted in U87EGFRwt cells. Western blots shown in j–l are representative of at least three independent replicates. Full-length blots are presented in Supplementary Figure 14. (m,n) Exogenous TNF protects GBM9 and GBM39 neurospheres from erlotinib-induced cell death. TNF (1 ng/ml) and erlotinib (1 µM) were added to cells concurrently and AlamarBlue cell viability assay was done after 72 h. (m) Erlotinib versus erlotinib + TNF: P = 0.0018, t = 7.41, d.f. = 4. (n) Erlotinib versus erlotinib + TNF: P = 0.0087, t = 4.79, d.f. = 4. Data are presented as mean ± s.e.m.; **P < 0.01, ***P < 0.001 from two-tailed unpaired Student’s t-test (n = 3 biologically independent experimental replicates).

Techniques Used: Inhibition, Viability Assay, Alamar Blue Assay, Control, Activation Assay, Western Blot, Two Tailed Test

Histone Deacetylase Assay:

Article Title: Sphingomyelin regulates astrocyte activity by regulating NF-κB signaling via HDAC1/3 expression
Article Snippet: Antibody to FLAG-M2 antibody (Cat# F1804) was purchased from Merck. .. Antibodies to p65 antibody (Cat# sc-8008), phospho-Ser 536 -p65 (Cat# sc-136548), TNF receptor 1 (TNFR1; Cat#sc-9436), histone deacetylase 1 (HDAC1; Cat# sc-81598), HDAC3 (Cat# sc-376957), calnexin (Cat# sc-46669), lamin B1 (Cat# sc-374015), and flotillin-1 (Cat# 74566) were obtained from Santa Cruz Biotechnology. .. The secondary antibodies used in this study were horseradish peroxidase-linked anti-rabbit IgG (Cat# 7074) and anti-mouse IgG (Cat# 7076) purchased from Cell Signaling Technology.

Article Title: Sphingomyelin regulates astrocyte activity by regulating NF-κB signaling via HDAC1/3 expression.
Article Snippet: Antibody to FLAG-M2 antibody (Cat# F1804) was purchased from Merck (Rahway, NJ, USA). .. Antibodies to p65 antibody (Cat# sc-8008), phospho-Ser536-p65 (Cat# sc-136548), TNF receptor 1 (TNFR1; Cat#sc9436), histone deacetylase 1 (HDAC1; Cat# sc-81598), HDAC3 (Cat# sc-376957), calnexin (Cat# sc-46669), lamin B1 (Cat# sc-374015), and flotillin-1 (Cat# 74566) were obtained from Santa Cruz Biotechnology (Dallas, TX, USA). .. The secondary antibodies used in this study were horseradish peroxidase-linked anti-rabbit IgG (Cat# 7074) and anti-mouse IgG (Cat# 7076) purchased from Cell Signaling Technology.

Incubation:

Article Title: Endothelial ADAM17 Promotes Neutrophil Migration and Pulmonary Microvascular Permeability in ARDS
Article Snippet: .. Sections were then incubated with primary antibodies targeting ADAM17 (rabbit anti-ADAM17, polyclonal, Bioss, USA), Ly6G/C (rat anti-Ly6G/C, clone RB6-8C5, Abcam, UK), VE-Cadherin (goat anti-VE-Cadherin, polyclonal, R&D Systems, USA), TNFR1 (mouse anti-TNFR1, clone H-5, Santa Cruz, USA), IL-6Rα (mouse anti-IL-6Rα, clone H-7, Santa Cruz, USA), and vWF (sheep anti-vWF, polyclonal, Abcam, UK) followed by incubation with the corresponding fluorescently labelled secondary antibodies including Alexa Fluor 488 goat anti-rabbit, Alexa Fluor 647 goat anti-rat, Alexa Fluor 488 donkey anti-goat, Alexa Fluor 594 goat anti-mouse, Alexa Fluor 488 donkey anti-mouse and Alexa Fluor 647 donkey anti-sheep. .. Nuclear counterstaining was performed using Roti-Mount FluorCare containing DAPI (4’,6-diamidino-2-phenylindole; HP20.1, Carl Roth, Germany).

Western Blot:

Article Title: Growth Hormone Effects on Hypoxia-Induced Neuroinflammation in the Developing Cerebellum
Article Snippet: CD206 , Rabbit/polyclonal , 1:1000 WB , Abcam , Ab64693. .. TNF-R1 , Goat/polyclonal , 1:1000 WB , Santa Cruz , sc-1068. .. TNF-R2 , Goat/polyclonal , 1:1000 WB , Santa Cruz , Sc-1072.

Article Title: Loss of ADAM17 in smooth muscle cells enhances their transformation to macrophage-like cells leading to more severe atherosclerosis in mice.
Article Snippet: Total protein concentration was determined with a BCA kit (BioRad). .. Western blotting was performed on aortic tissue, SMC or macrophage protein extracts as before [7] using the following antibodies: CD68 (BioRad), Calponin 1 (Abcam), ADAM17 (Sigma for human, Kerafast for mouse), Caspase 3 (Cell Signaling), αSMA (Abcam), Galectin 3 (Abcam), SM22α/Transgelin (Abcam), ABCA1 (Novus Bio), CD36 (Novus Bio), SR-A1 (Novus Bio), LAL (Abcam), TNFR1 (Santa Cruz), TNFR2 (Cell Signaling), LXR (Abcam), NFκB (p65) (Santa Cruz), Phospho- and total IKKα/β (Cell Signaling). .. The intensity of bands on immunoblots was quantified using the Image-Quant TL software (Cytiva), and normalized to total protein (memcode-stained membrane).

Review