rabbit anti solute carrier family 7 member 11 Search Results


93
Alomone Labs cystine glutamate antiporter
AhR activation status does not affect Nrf2 activation or transcriptional activity. RPTECs were cultured under ctrl conditions or subjected to Reox with or without the AhR inhibitor CH223191. (A) Representative western blots of Nrf2 levels (corresponding to its activation status) and the expression of the Nrf2 transcriptional targets xCT <t>(SLC7A11)</t> and SOD-3. (B-D) Statistical analysis of the western blots. Neither Reox nor CH223191 affects Nrf2 activity, or the expression of xCT and SOD-3. Data are presented as the mean ± SEM of six independent experiments. AhR, arylhydrocarbon receptor; Nrf2, nuclear factor erythroid 2-related factor 2; xCT, cystine-glutamate <t>antiporter;</t> SOD-3, superoxide dismutase; RPTEC, renal proximal tubular epithelial cell; ctrl, control; Reox, reoxygenation.
Cystine Glutamate Antiporter, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Novus Biologicals rabbit anti slc7a7
AhR activation status does not affect Nrf2 activation or transcriptional activity. RPTECs were cultured under ctrl conditions or subjected to Reox with or without the AhR inhibitor CH223191. (A) Representative western blots of Nrf2 levels (corresponding to its activation status) and the expression of the Nrf2 transcriptional targets xCT <t>(SLC7A11)</t> and SOD-3. (B-D) Statistical analysis of the western blots. Neither Reox nor CH223191 affects Nrf2 activity, or the expression of xCT and SOD-3. Data are presented as the mean ± SEM of six independent experiments. AhR, arylhydrocarbon receptor; Nrf2, nuclear factor erythroid 2-related factor 2; xCT, cystine-glutamate <t>antiporter;</t> SOD-3, superoxide dismutase; RPTEC, renal proximal tubular epithelial cell; ctrl, control; Reox, reoxygenation.
Rabbit Anti Slc7a7, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Cell Signaling Technology Inc slc7a5
Control of <t>Slc7a5</t> expression. ( A ) Western blot for SLC7A5 following control or SLC7A5 plasmid transfection of Neuro-2a cells ( N = 6, 6). ( B ) Western blot for myc from lysates of Neuro-2a cells transfected with control, myc-Slc7a5 and control, or myc-Slc7a5 and Slc7a5 shRNA plasmids ( N = 3, 3, 3). ( C ) Schematic diagram representing a sagittal section of the mouse brain. The diagram depicts electroporated (red) NSCs surrounding the LVs that generate neuroblasts that migrate through the RMS and enter into the OB 7 days post-electroporation and become mature GCs 30 days post-electroporation. ( D and E ) ×20 image of RFP+ cells co-electroporated with SLC7A5 in the SVZ and stained for SLC7A5. Scalebar = 50 μm. ( F – K ) ×5 images of P14 and P30 SVZs following P0 co-electroporation with RFP and control, shSlc7a5, or SLC7A5 plasmids. P14 control, N = 6; shSlc7a5, N = 6; or SLC7A5, N = 3. P30 control, N = 7; shSlc7a5, N = 8; or SLC7A5, N = 4 scalebar = 100 μm. ( L ) Quantification of F–K.
Slc7a5, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Boster Bio anti slc7a5
Control of <t>Slc7a5</t> expression. ( A ) Western blot for SLC7A5 following control or SLC7A5 plasmid transfection of Neuro-2a cells ( N = 6, 6). ( B ) Western blot for myc from lysates of Neuro-2a cells transfected with control, myc-Slc7a5 and control, or myc-Slc7a5 and Slc7a5 shRNA plasmids ( N = 3, 3, 3). ( C ) Schematic diagram representing a sagittal section of the mouse brain. The diagram depicts electroporated (red) NSCs surrounding the LVs that generate neuroblasts that migrate through the RMS and enter into the OB 7 days post-electroporation and become mature GCs 30 days post-electroporation. ( D and E ) ×20 image of RFP+ cells co-electroporated with SLC7A5 in the SVZ and stained for SLC7A5. Scalebar = 50 μm. ( F – K ) ×5 images of P14 and P30 SVZs following P0 co-electroporation with RFP and control, shSlc7a5, or SLC7A5 plasmids. P14 control, N = 6; shSlc7a5, N = 6; or SLC7A5, N = 3. P30 control, N = 7; shSlc7a5, N = 8; or SLC7A5, N = 4 scalebar = 100 μm. ( L ) Quantification of F–K.
Anti Slc7a5, supplied by Boster Bio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc rabbit polyclonal anti slc7a5 antibody
Prediction of target gene of 7 miRNAs screened by miRNAmicroassay
Rabbit Polyclonal Anti Slc7a5 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Millipore rabbit anti-rnase 7 antibody
To confirm the mRNA expression of RNH1 and RNASE7 pattern is accompanied by alterations in peptide production, ELISA quantitated RI and <t>RNase</t> <t>7</t> peptide from the same non-infected kidney tissue and kidney tissue with pyelonephritis used in real-time PCR analysis. RI production significantly decreased with pyelonephritis ( p =0.0068) while RNase 7 expression significantly increased ( p =0.0386).
Rabbit Anti Rnase 7 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Danaher Inc rabbit anti slc7a5 lat1 antibody
To confirm the mRNA expression of RNH1 and RNASE7 pattern is accompanied by alterations in peptide production, ELISA quantitated RI and <t>RNase</t> <t>7</t> peptide from the same non-infected kidney tissue and kidney tissue with pyelonephritis used in real-time PCR analysis. RI production significantly decreased with pyelonephritis ( p =0.0068) while RNase 7 expression significantly increased ( p =0.0386).
Rabbit Anti Slc7a5 Lat1 Antibody, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Cell Signaling Technology Inc solute carrier family 7 member 11
To confirm the mRNA expression of RNH1 and RNASE7 pattern is accompanied by alterations in peptide production, ELISA quantitated RI and <t>RNase</t> <t>7</t> peptide from the same non-infected kidney tissue and kidney tissue with pyelonephritis used in real-time PCR analysis. RI production significantly decreased with pyelonephritis ( p =0.0068) while RNase 7 expression significantly increased ( p =0.0386).
Solute Carrier Family 7 Member 11, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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97
Cell Signaling Technology Inc anti soluble carrier family 7 member 11 slc7a11
TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; <t>Slc7a11,</t> soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.
Anti Soluble Carrier Family 7 Member 11 Slc7a11, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Alomone Labs amino acids
TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; <t>Slc7a11,</t> soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.
Amino Acids, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Bio-Rad anti human cd98
TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; <t>Slc7a11,</t> soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.
Anti Human Cd98, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Proteintech anti slc7a5
TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; <t>Slc7a11,</t> soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.
Anti Slc7a5, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


AhR activation status does not affect Nrf2 activation or transcriptional activity. RPTECs were cultured under ctrl conditions or subjected to Reox with or without the AhR inhibitor CH223191. (A) Representative western blots of Nrf2 levels (corresponding to its activation status) and the expression of the Nrf2 transcriptional targets xCT (SLC7A11) and SOD-3. (B-D) Statistical analysis of the western blots. Neither Reox nor CH223191 affects Nrf2 activity, or the expression of xCT and SOD-3. Data are presented as the mean ± SEM of six independent experiments. AhR, arylhydrocarbon receptor; Nrf2, nuclear factor erythroid 2-related factor 2; xCT, cystine-glutamate antiporter; SOD-3, superoxide dismutase; RPTEC, renal proximal tubular epithelial cell; ctrl, control; Reox, reoxygenation.

Journal: Molecular Medicine Reports

Article Title: Reoxygenation induces reactive oxygen species production and ferroptosis in renal tubular epithelial cells by activating aryl hydrocarbon receptor

doi: 10.3892/mmr.2020.11679

Figure Lengend Snippet: AhR activation status does not affect Nrf2 activation or transcriptional activity. RPTECs were cultured under ctrl conditions or subjected to Reox with or without the AhR inhibitor CH223191. (A) Representative western blots of Nrf2 levels (corresponding to its activation status) and the expression of the Nrf2 transcriptional targets xCT (SLC7A11) and SOD-3. (B-D) Statistical analysis of the western blots. Neither Reox nor CH223191 affects Nrf2 activity, or the expression of xCT and SOD-3. Data are presented as the mean ± SEM of six independent experiments. AhR, arylhydrocarbon receptor; Nrf2, nuclear factor erythroid 2-related factor 2; xCT, cystine-glutamate antiporter; SOD-3, superoxide dismutase; RPTEC, renal proximal tubular epithelial cell; ctrl, control; Reox, reoxygenation.

Article Snippet: Primary antibodies were specific for AhR (1:200; cat. no. sc-133088; Santa Cruz Biotechnology, Inc.), cytochrome P450 family 1 subfamily A member 1 (CYP1A1; 1:500; cat. no. sc-25304; Santa Cruz Biotechnology, Inc.), Nrf2 (1:1,000; cat. no. TA343586; OriGene Technologies, Inc.), superoxide dismutase 3 (SOD-3; 1:100; cat. no. sc-271170; Santa Cruz Biotechnology, Inc.), cystine-glutamate antiporter (xCT, also known as SLC7A11; 1:1,000; cat. no. ANT-111; Alomone Labs), HIF-1α (1:500; cat. no. sc-10790; Santa Cruz Biotechnology, Inc.), LDH-A (1:1,000; cat. no. 2012; Cell Signaling Technology, Inc.), activated cleaved caspase-3 (CC3; 1:1,000; cat. no. ab13847; Abcam) and β-actin (1:2,500; cat. no. 4967; Cell Signaling Technology, Inc.).

Techniques: Activation Assay, Activity Assay, Cell Culture, Western Blot, Expressing

Control of Slc7a5 expression. ( A ) Western blot for SLC7A5 following control or SLC7A5 plasmid transfection of Neuro-2a cells ( N = 6, 6). ( B ) Western blot for myc from lysates of Neuro-2a cells transfected with control, myc-Slc7a5 and control, or myc-Slc7a5 and Slc7a5 shRNA plasmids ( N = 3, 3, 3). ( C ) Schematic diagram representing a sagittal section of the mouse brain. The diagram depicts electroporated (red) NSCs surrounding the LVs that generate neuroblasts that migrate through the RMS and enter into the OB 7 days post-electroporation and become mature GCs 30 days post-electroporation. ( D and E ) ×20 image of RFP+ cells co-electroporated with SLC7A5 in the SVZ and stained for SLC7A5. Scalebar = 50 μm. ( F – K ) ×5 images of P14 and P30 SVZs following P0 co-electroporation with RFP and control, shSlc7a5, or SLC7A5 plasmids. P14 control, N = 6; shSlc7a5, N = 6; or SLC7A5, N = 3. P30 control, N = 7; shSlc7a5, N = 8; or SLC7A5, N = 4 scalebar = 100 μm. ( L ) Quantification of F–K.

Journal: Human Molecular Genetics

Article Title: The amino acid transporter Slc7a5 regulates the mTOR pathway and is required for granule cell development

doi: 10.1093/hmg/ddaa186

Figure Lengend Snippet: Control of Slc7a5 expression. ( A ) Western blot for SLC7A5 following control or SLC7A5 plasmid transfection of Neuro-2a cells ( N = 6, 6). ( B ) Western blot for myc from lysates of Neuro-2a cells transfected with control, myc-Slc7a5 and control, or myc-Slc7a5 and Slc7a5 shRNA plasmids ( N = 3, 3, 3). ( C ) Schematic diagram representing a sagittal section of the mouse brain. The diagram depicts electroporated (red) NSCs surrounding the LVs that generate neuroblasts that migrate through the RMS and enter into the OB 7 days post-electroporation and become mature GCs 30 days post-electroporation. ( D and E ) ×20 image of RFP+ cells co-electroporated with SLC7A5 in the SVZ and stained for SLC7A5. Scalebar = 50 μm. ( F – K ) ×5 images of P14 and P30 SVZs following P0 co-electroporation with RFP and control, shSlc7a5, or SLC7A5 plasmids. P14 control, N = 6; shSlc7a5, N = 6; or SLC7A5, N = 3. P30 control, N = 7; shSlc7a5, N = 8; or SLC7A5, N = 4 scalebar = 100 μm. ( L ) Quantification of F–K.

Article Snippet: Free-floating sections were blocked in PBS containing 0.1% Triton X-100, 0.1% Tween-20 and 2% BSA and incubated in primary antibody pS6 (rabbit anti-pS6; 1:1000; cell signaling technology; Ser 240/244, 61H9, #4838), or SLC7A5 (rabbit anti-SLC7A5; 1:1000; Cell Signaling Technology; #5347) overnight at 4°C.

Techniques: Control, Expressing, Western Blot, Plasmid Preparation, Transfection, shRNA, Electroporation, Staining

Slc7a5 is required for GC dendrite morphology. ( A – C ) ×20 images of P14 OB GCs from P0 electroporation of RFP and control, shSlc7a5, or SLC7A5 plasmids. ( D ) Sholl analysis of A-C. P14 control, N = 6, n = 44; shSlc7a5, N = 4, n = 58; SLC7A5, N = 3, n = 23. ( E ) Total number of crossings per GC for A-C. ( F–H ) ×20 images of P30 GCs from P0 electroporation of RFP and control, shSlc7a5 or SLC7A5 plasmids. ( I ) Sholl analysis of F–H. P30 control, N = 4, n = 38; shSlc7a5, N = 3, n = 46; SLC7A5, N = 4, n = 37. ( J ) Total number of crossings per GC for F–H. Scalebar = 50 μm. **** = P < 0.0001.

Journal: Human Molecular Genetics

Article Title: The amino acid transporter Slc7a5 regulates the mTOR pathway and is required for granule cell development

doi: 10.1093/hmg/ddaa186

Figure Lengend Snippet: Slc7a5 is required for GC dendrite morphology. ( A – C ) ×20 images of P14 OB GCs from P0 electroporation of RFP and control, shSlc7a5, or SLC7A5 plasmids. ( D ) Sholl analysis of A-C. P14 control, N = 6, n = 44; shSlc7a5, N = 4, n = 58; SLC7A5, N = 3, n = 23. ( E ) Total number of crossings per GC for A-C. ( F–H ) ×20 images of P30 GCs from P0 electroporation of RFP and control, shSlc7a5 or SLC7A5 plasmids. ( I ) Sholl analysis of F–H. P30 control, N = 4, n = 38; shSlc7a5, N = 3, n = 46; SLC7A5, N = 4, n = 37. ( J ) Total number of crossings per GC for F–H. Scalebar = 50 μm. **** = P < 0.0001.

Article Snippet: Free-floating sections were blocked in PBS containing 0.1% Triton X-100, 0.1% Tween-20 and 2% BSA and incubated in primary antibody pS6 (rabbit anti-pS6; 1:1000; cell signaling technology; Ser 240/244, 61H9, #4838), or SLC7A5 (rabbit anti-SLC7A5; 1:1000; Cell Signaling Technology; #5347) overnight at 4°C.

Techniques: Electroporation, Control

Slc7a5 is required for GC survival. ( A and B ) ×5 images of P14 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( C ) Relative number of RFP+ GCs at P14 for control or shSlc7a5 conditions. P14 control, N = 6; shSlc7a5, N = 6. ( D and E ) ×5 images of P30 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( F ) Relative number of RFP+ GCs at P30 for control or shSlc7a5 conditions. P30 control, N = 7; shSlc7a5, N = 8. ( G and H ) ×5 images of P70 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( I ) Relative number of RFP+ GCs at P30 for control or shSlc7a5 conditions. P70 control, N = 4; shSlc7a5, N = 3. Scalebar = 100 μm. **** = P < 0.0001.

Journal: Human Molecular Genetics

Article Title: The amino acid transporter Slc7a5 regulates the mTOR pathway and is required for granule cell development

doi: 10.1093/hmg/ddaa186

Figure Lengend Snippet: Slc7a5 is required for GC survival. ( A and B ) ×5 images of P14 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( C ) Relative number of RFP+ GCs at P14 for control or shSlc7a5 conditions. P14 control, N = 6; shSlc7a5, N = 6. ( D and E ) ×5 images of P30 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( F ) Relative number of RFP+ GCs at P30 for control or shSlc7a5 conditions. P30 control, N = 7; shSlc7a5, N = 8. ( G and H ) ×5 images of P70 Obs from P0 electroporation of RFP and control or shSlc7a5 plasmids. ( I ) Relative number of RFP+ GCs at P30 for control or shSlc7a5 conditions. P70 control, N = 4; shSlc7a5, N = 3. Scalebar = 100 μm. **** = P < 0.0001.

Article Snippet: Free-floating sections were blocked in PBS containing 0.1% Triton X-100, 0.1% Tween-20 and 2% BSA and incubated in primary antibody pS6 (rabbit anti-pS6; 1:1000; cell signaling technology; Ser 240/244, 61H9, #4838), or SLC7A5 (rabbit anti-SLC7A5; 1:1000; Cell Signaling Technology; #5347) overnight at 4°C.

Techniques: Electroporation, Control

Slc7a5 regulation of dendrite morphology depends on mTOR pathway activity. ( A ) Images of P30 GCs from RFP and control, shSlc7a5, Rheb or shSlc7a5 with Rheb plasmids, stained for pS6. Scalebar = 12.5 μm. ( B ) The quantification of pS6 staining intensity for A. control, N = 3, n = 39; shSlc7a5, N = 5, n = 33; Rheb, N = 3, n = 37; shSlc7a5 and Rheb, N = 5, n = 60. ( C–F ) ×20 images of P30 GCs from P0 electroporation of RFP and control, shSlc7a5, Rheb, or shSlc7a5 and Rheb plasmids. Scalebar = 50 μm. ( G ) Sholl analysis for C-F. ( H ) Total number of crossings per GC for C-F. control, N = 3, n = 23; shSlc7a5, N = 4, n = 35; Rheb, N = 5, n = 32; shSlc7a5 and Rheb, N = 5, n = 47. *** = P < 0.001. **** = P < 0.0001.

Journal: Human Molecular Genetics

Article Title: The amino acid transporter Slc7a5 regulates the mTOR pathway and is required for granule cell development

doi: 10.1093/hmg/ddaa186

Figure Lengend Snippet: Slc7a5 regulation of dendrite morphology depends on mTOR pathway activity. ( A ) Images of P30 GCs from RFP and control, shSlc7a5, Rheb or shSlc7a5 with Rheb plasmids, stained for pS6. Scalebar = 12.5 μm. ( B ) The quantification of pS6 staining intensity for A. control, N = 3, n = 39; shSlc7a5, N = 5, n = 33; Rheb, N = 3, n = 37; shSlc7a5 and Rheb, N = 5, n = 60. ( C–F ) ×20 images of P30 GCs from P0 electroporation of RFP and control, shSlc7a5, Rheb, or shSlc7a5 and Rheb plasmids. Scalebar = 50 μm. ( G ) Sholl analysis for C-F. ( H ) Total number of crossings per GC for C-F. control, N = 3, n = 23; shSlc7a5, N = 4, n = 35; Rheb, N = 5, n = 32; shSlc7a5 and Rheb, N = 5, n = 47. *** = P < 0.001. **** = P < 0.0001.

Article Snippet: Free-floating sections were blocked in PBS containing 0.1% Triton X-100, 0.1% Tween-20 and 2% BSA and incubated in primary antibody pS6 (rabbit anti-pS6; 1:1000; cell signaling technology; Ser 240/244, 61H9, #4838), or SLC7A5 (rabbit anti-SLC7A5; 1:1000; Cell Signaling Technology; #5347) overnight at 4°C.

Techniques: Activity Assay, Control, Staining, Electroporation

Prediction of target gene of 7 miRNAs screened by miRNAmicroassay

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: Prediction of target gene of 7 miRNAs screened by miRNAmicroassay

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques:

The protein expression was further confirmed by Western blot analysis after three days of transfection. The levels of the SLC7A5 protein were significantly lower in SLC7A5-siRNA group than in the negative control group and Mock. In comparison, GAPDH protein did not vary markedly among the three groups.

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: The protein expression was further confirmed by Western blot analysis after three days of transfection. The levels of the SLC7A5 protein were significantly lower in SLC7A5-siRNA group than in the negative control group and Mock. In comparison, GAPDH protein did not vary markedly among the three groups.

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques: Expressing, Western Blot, Transfection, Negative Control, Comparison

Cell proliferation of SKM-1 cells using CCK-8 assays. The growth of SKM-1 cells in SLC7A5-siRNA group was significantly inhibited compared with the negative control (NC) group ( P <0.05).

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: Cell proliferation of SKM-1 cells using CCK-8 assays. The growth of SKM-1 cells in SLC7A5-siRNA group was significantly inhibited compared with the negative control (NC) group ( P <0.05).

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques: CCK-8 Assay, Negative Control

Cell apoptosis analysis of SLC7A5-siRNA group and negative control group cells was analyzed by flow cytometry. A. Representative histograms of annexin V/PI double-staining flow cytometry. B. Percent apoptosis (including early and late apoptotic cells) determined by flow cytometry (n = 3). * P <0.05 vs control.

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: Cell apoptosis analysis of SLC7A5-siRNA group and negative control group cells was analyzed by flow cytometry. A. Representative histograms of annexin V/PI double-staining flow cytometry. B. Percent apoptosis (including early and late apoptotic cells) determined by flow cytometry (n = 3). * P <0.05 vs control.

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques: Negative Control, Flow Cytometry, Double Staining, Control

Cell cycle assay by flow cytometry in  SLC7A5-siRNAand  negative control group

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: Cell cycle assay by flow cytometry in SLC7A5-siRNAand negative control group

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques: Cell Cycle Assay, Flow Cytometry, Negative Control

Cell cycle distribution of SLC7A5-siRNA group and negative control group cells was analyzed by flow cytometry with PI staining after 48 h treatment. A. Representative flow cytometry histograms. B. Cell distribution at G0/G1, S, and G2/M phases of the cell cycle (n = 3). * P <0.05 vs control.

Journal: Oncotarget

Article Title: SLC7A5 act as a potential leukemic transformation target gene in myelodysplastic syndrome

doi: 10.18632/oncotarget.6512

Figure Lengend Snippet: Cell cycle distribution of SLC7A5-siRNA group and negative control group cells was analyzed by flow cytometry with PI staining after 48 h treatment. A. Representative flow cytometry histograms. B. Cell distribution at G0/G1, S, and G2/M phases of the cell cycle (n = 3). * P <0.05 vs control.

Article Snippet: The antibodies, used for Western blot analysis, included rabbit polyclonal anti-SLC7A5 antibody (Cell signaling tech Inc., 1:1000), anti-GAPDH antibody (Kangchen Inc., 1:10000), and HRP-conjugated anti-rabbit secondary antibody (Kangchen Inc., 1:10000).

Techniques: Negative Control, Flow Cytometry, Staining, Control

To confirm the mRNA expression of RNH1 and RNASE7 pattern is accompanied by alterations in peptide production, ELISA quantitated RI and RNase 7 peptide from the same non-infected kidney tissue and kidney tissue with pyelonephritis used in real-time PCR analysis. RI production significantly decreased with pyelonephritis ( p =0.0068) while RNase 7 expression significantly increased ( p =0.0386).

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: To confirm the mRNA expression of RNH1 and RNASE7 pattern is accompanied by alterations in peptide production, ELISA quantitated RI and RNase 7 peptide from the same non-infected kidney tissue and kidney tissue with pyelonephritis used in real-time PCR analysis. RI production significantly decreased with pyelonephritis ( p =0.0068) while RNase 7 expression significantly increased ( p =0.0386).

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Infection, Real-time Polymerase Chain Reaction

( A ) Human kidney was labeled RNase 7 (green/arrows), aquaporin-2 (AQP-2/red), and nuclei (blue). Principal cells, identified by AQP-2 positive staining, were negative for RNase 7. ( B ) Human kidney was labeled with RNase 7 (green/arrows), RI (red/arrowheads), and nuclei (blue). RNase 7 positive cells/intercalated cells express RI. Magnification 100x.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: ( A ) Human kidney was labeled RNase 7 (green/arrows), aquaporin-2 (AQP-2/red), and nuclei (blue). Principal cells, identified by AQP-2 positive staining, were negative for RNase 7. ( B ) Human kidney was labeled with RNase 7 (green/arrows), RI (red/arrowheads), and nuclei (blue). RNase 7 positive cells/intercalated cells express RI. Magnification 100x.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Labeling, Staining

( A ) Representative silver stained SDS-PAGE gels demonstrating recombinant RI proteolysis by the neutrophil proteases neutrophil elastase (NE) and proteinase 3 (Pr3). Lane 1: molecular weight marker (MW), Lane 2: 3 μg recombinant RI without proteases, Lane 3: RI incubated with 100ng NE, Lane 4–6: recombinant RI incubated with 6ng, 30ng, and 60ng Pr3, respectively. ( B/C ) Clinical urine isolates infected with E. coli were incubated with and without protease inhibitor cocktail (PI) and subjected to SDS-PAGE followed by Western immunoblot analysis using a monoclonal antibody directed against RI or a polyclonal antibody directed against RNase 7. (B) Results demonstrate that urine proteases degrade urinary RI and protease inhibitor cocktail prevents RI proteolysis. (C) Urinary proteases did not cause significant RNase 7 degradation. 50ng recombinant RI or RNase 7 served as control.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: ( A ) Representative silver stained SDS-PAGE gels demonstrating recombinant RI proteolysis by the neutrophil proteases neutrophil elastase (NE) and proteinase 3 (Pr3). Lane 1: molecular weight marker (MW), Lane 2: 3 μg recombinant RI without proteases, Lane 3: RI incubated with 100ng NE, Lane 4–6: recombinant RI incubated with 6ng, 30ng, and 60ng Pr3, respectively. ( B/C ) Clinical urine isolates infected with E. coli were incubated with and without protease inhibitor cocktail (PI) and subjected to SDS-PAGE followed by Western immunoblot analysis using a monoclonal antibody directed against RI or a polyclonal antibody directed against RNase 7. (B) Results demonstrate that urine proteases degrade urinary RI and protease inhibitor cocktail prevents RI proteolysis. (C) Urinary proteases did not cause significant RNase 7 degradation. 50ng recombinant RI or RNase 7 served as control.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Staining, SDS Page, Recombinant, Molecular Weight, Marker, Incubation, Infection, Protease Inhibitor, Western Blot

( A ) Binding of recombinant RNase 7 to RI was confirmed by native gel electrophoresis. Representative native gels demonstrate a mobility shift in recombinant RI upon RNase 7 binding as visualized by silver-staining. Results also show that the interaction of RI with RNase 7 can be blocked by pre-incubation with the RI inhibitor p -HMB. ( B ) Binding of endogenous RNase 7 to RI was confirmed using co-immunoprecipitation assays. Lysates of human bladder (B), non-infected kidney tissue (Nl), and kidney tissue with pyelonephritis (P) were immunoprecipitated with anti-RI monoclonal antibody, subjected to SDS-PAGE, followed by Western immunoblot analysis using anti-RNase 7 polyclonal antibody. Results indicate that RNase 7 complexes with RI in human bladder and kidney tissue. 25ng recombinant RNase 7 served as control. ( C ) Urinary RI from non-infected urine (NI) and urine infected with E. coli (I) was pulled down using recombinant RNase 7 and subjected to SDS-PAGE followed by Western immunoblot analysis using anti-RI monoclonal antibody. Results demonstrate that urinary RI in infected urine binds recombinant RNase 7. 50ng recombinant RI served as control.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: ( A ) Binding of recombinant RNase 7 to RI was confirmed by native gel electrophoresis. Representative native gels demonstrate a mobility shift in recombinant RI upon RNase 7 binding as visualized by silver-staining. Results also show that the interaction of RI with RNase 7 can be blocked by pre-incubation with the RI inhibitor p -HMB. ( B ) Binding of endogenous RNase 7 to RI was confirmed using co-immunoprecipitation assays. Lysates of human bladder (B), non-infected kidney tissue (Nl), and kidney tissue with pyelonephritis (P) were immunoprecipitated with anti-RI monoclonal antibody, subjected to SDS-PAGE, followed by Western immunoblot analysis using anti-RNase 7 polyclonal antibody. Results indicate that RNase 7 complexes with RI in human bladder and kidney tissue. 25ng recombinant RNase 7 served as control. ( C ) Urinary RI from non-infected urine (NI) and urine infected with E. coli (I) was pulled down using recombinant RNase 7 and subjected to SDS-PAGE followed by Western immunoblot analysis using anti-RI monoclonal antibody. Results demonstrate that urinary RI in infected urine binds recombinant RNase 7. 50ng recombinant RI served as control.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Binding Assay, Recombinant, Nucleic Acid Electrophoresis, Mobility Shift, Silver Staining, Incubation, Immunoprecipitation, Infection, SDS Page, Western Blot

( A ) Uropathogenic E. coli was exposed to 2 μM RNase 7, equal concentrations of recombinant RNase 7 pre-incubated with RI (RNase 7-RI), or 2 μM of RI. Untreated bacteria served as the control. The results are displayed as the percentage of remaining CFUs in relation to untreated controls. The antimicrobial activity of RNase 7 was significantly reduced in the presence of RI. Data represent the mean of triplicates ± SEM. ( B ) E. coli were stained using a 1:1 mixture of SYTO9 and propidium iodide. The SYTO9-stained cells (green) represent live cells and the propidium iodide-stained cells (red) represent killed cells. Bacterial viability was visualized after exposure to RNase 7 with and without RI at 180 minutes. Magnification 63x. (C) E. coli were stained using a 1:1 mixture of SYTO9 and propidium iodide and incubated with 2 μM RNase 7, equal concentrations of recombinant RNase 7 pre-incubated with RI (RNase 7-RI), or 2 μM of RI. Bacterial viability over time was analyzed integrating fluorescent changes in SYTO9 and propidium iodide dye. Values are the average of three replicates.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: ( A ) Uropathogenic E. coli was exposed to 2 μM RNase 7, equal concentrations of recombinant RNase 7 pre-incubated with RI (RNase 7-RI), or 2 μM of RI. Untreated bacteria served as the control. The results are displayed as the percentage of remaining CFUs in relation to untreated controls. The antimicrobial activity of RNase 7 was significantly reduced in the presence of RI. Data represent the mean of triplicates ± SEM. ( B ) E. coli were stained using a 1:1 mixture of SYTO9 and propidium iodide. The SYTO9-stained cells (green) represent live cells and the propidium iodide-stained cells (red) represent killed cells. Bacterial viability was visualized after exposure to RNase 7 with and without RI at 180 minutes. Magnification 63x. (C) E. coli were stained using a 1:1 mixture of SYTO9 and propidium iodide and incubated with 2 μM RNase 7, equal concentrations of recombinant RNase 7 pre-incubated with RI (RNase 7-RI), or 2 μM of RI. Bacterial viability over time was analyzed integrating fluorescent changes in SYTO9 and propidium iodide dye. Values are the average of three replicates.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Recombinant, Incubation, Activity Assay, Staining

The antimicrobial properties of urinary RNase 7 were measured as changes in turbidity of cultured human urine using the absorbance at 600 nm (OD 600 ). Human urine samples were inoculated with E. coli (PEDUTI-89 or CFT073) as shown by the dashed line. Addition of RI (solid black line) or RNase 7 monoclonal antibody (diamond studded line) blocked the antimicrobial activity of RNase 7, resulting in increased bacterial growth. The open circles represent non-inoculated urine samples.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: The antimicrobial properties of urinary RNase 7 were measured as changes in turbidity of cultured human urine using the absorbance at 600 nm (OD 600 ). Human urine samples were inoculated with E. coli (PEDUTI-89 or CFT073) as shown by the dashed line. Addition of RI (solid black line) or RNase 7 monoclonal antibody (diamond studded line) blocked the antimicrobial activity of RNase 7, resulting in increased bacterial growth. The open circles represent non-inoculated urine samples.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Cell Culture, Activity Assay

( A ) To determine if RI alters RNase 7 bacterial binding, E. coli were incubated with 2 μM RNase 7 (R7), RNase 7 pre-incubated with RI (R7/RI), or 2 μM RI alone. After centrifugation, the supernatant and pellet fraction were subjected to SDS-PAGE and visualized by Coomassie Blue staining. Supernatant represents the soluble fraction that contains unbound protein while the pellet fraction contains the E.coli -bound peptides. Results demonstrate that RNase 7 binds uropathogenic E. coli (E) and that binding is reduced in the presence of RI. ( B ) Displacement of LPS-bound Bodipy TR cadavarine with increasing concentrations of RNase 7, Polymyxin B, RNase A, and RI. Results confirm that RNase 7 binds LPS while RI does not. ( C ) Displacement of LPS-bound Bodipy TR cadavarine with increasing concentrations of RI pre-incubated with 1 μM RNase 7. Results confirm that the addition of RI reduces RNase 7 binding to LPS. The addition of p -HMB to RI improves RNase 7 binding to LPS.

Journal: Kidney international

Article Title: An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract

doi: 10.1038/ki.2013.395

Figure Lengend Snippet: ( A ) To determine if RI alters RNase 7 bacterial binding, E. coli were incubated with 2 μM RNase 7 (R7), RNase 7 pre-incubated with RI (R7/RI), or 2 μM RI alone. After centrifugation, the supernatant and pellet fraction were subjected to SDS-PAGE and visualized by Coomassie Blue staining. Supernatant represents the soluble fraction that contains unbound protein while the pellet fraction contains the E.coli -bound peptides. Results demonstrate that RNase 7 binds uropathogenic E. coli (E) and that binding is reduced in the presence of RI. ( B ) Displacement of LPS-bound Bodipy TR cadavarine with increasing concentrations of RNase 7, Polymyxin B, RNase A, and RI. Results confirm that RNase 7 binds LPS while RI does not. ( C ) Displacement of LPS-bound Bodipy TR cadavarine with increasing concentrations of RI pre-incubated with 1 μM RNase 7. Results confirm that the addition of RI reduces RNase 7 binding to LPS. The addition of p -HMB to RI improves RNase 7 binding to LPS.

Article Snippet: Samples were loaded on SDS-PAGE followed by Western immunoblot analysis using rabbit anti-RNase 7 antibody (Sigma-Aldrich).

Techniques: Binding Assay, Incubation, Centrifugation, SDS Page, Staining

TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control

TNF, tumor necrosis factor; Con, control (untreated); Desi, desipramine; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; ER, endoplasmic reticulum. * P < 0.05, ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: TNF, tumor necrosis factor; Con, control (untreated); Desi, desipramine; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; ER, endoplasmic reticulum. * P < 0.05, ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control

Con, control (untreated); PB, Protaetia brevitarsis ; Desi, desipramine; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; GSH, glutathione; MDA, malondialdehyde; TNF, tumor necrosis factor. * P < 0.05, ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: Con, control (untreated); PB, Protaetia brevitarsis ; Desi, desipramine; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; GSH, glutathione; MDA, malondialdehyde; TNF, tumor necrosis factor. * P < 0.05, ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control

TNF, tumor necrosis factor; Con, control (untreated); LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; ERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; NF, nuclear factor. ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: TNF, tumor necrosis factor; Con, control (untreated); LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; ERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4; NF, nuclear factor. ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control

TNF, tumor necrosis factor; Con, control (untreated); NAC, N-acetylcysteine; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; GPX4, glutathione peroxidase 4; Slc7a11, soluble carrier family 7 member 11; ER, endoplasmic reticulum. ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: TNF, tumor necrosis factor; Con, control (untreated); NAC, N-acetylcysteine; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; GPX4, glutathione peroxidase 4; Slc7a11, soluble carrier family 7 member 11; ER, endoplasmic reticulum. ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control

TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; ASMase, acid sphingomyelinase; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.

Journal: Nutrition Research and Practice

Article Title: Protaetia brevitarsis larvae extract protects against lipopolysaccharides-induced ferroptosis and inflammation by inhibiting acid sphingomyelinase

doi: 10.4162/nrp.2024.18.5.602

Figure Lengend Snippet: TNF, tumor necrosis factor; Con, control (untreated); PB, Protaetia brevitarsis ; LPS, lipopolysaccharides; IL, interleukin; GSH, glutathione; MDA, malondialdehyde; ASMase, acid sphingomyelinase; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2A; Slc7a11, soluble carrier family 7 member 11; GPX4, glutathione peroxidase 4. * P < 0.05, ** P < 0.01, *** P < 0.001.

Article Snippet: Anti-cleaved caspase-3 (9664), anti-phospho-protein kinase R-like endoplasmic reticulum kinase (PERK) (Thr980) (3179), anti-phospho-eukaryotic translation initiation factor 2A (eIF2α) (Ser51) (3597), anti-phospho-SAPK/JNK (Thr183/Tyr185) (9255), anti-phospho-p38 (Thr180/Tyr182) (4511), anti-phospho-p65 (Ser536) (3033), anti-soluble carrier family 7 member 11 (Slc7a11) (12691), and anti-GPX4 (59735) antibodies were purchased from Cell Signaling Technology (Beverly, MA).

Techniques: Control