polyclonal antibodies against adipocyte differentiation-related protein (adrp) Search Results


91
Thermo Fisher gene exp plin2 hs00605340 m1
Oleic acid (C18:1)-induced vanin-1 mRNA expression during the course of lipid accumulation in HuH-7 cells. (A) Immunofluorescence to show lipid accumulation (green) and nuclei (blue) in human hepatoma cell line HuH-7. After 24-h induction with 0 (control), 0.01, 0.1, 1, and 2 mM oleic acid, HuH-7 cells were fixed and observed by confocal laser-scanning microscopy. Note the absence of green fluorescence at oleic acid concentrations of 0.01 and 0.1 mM. (B)–(D) Relative expressions of vanin-1 (B), PPARα (C), and <t>ADRP</t> (D) in HuH-7 cells with the same doses of oleic acid. The values shown are the mean (SEM) ( n = 6); *** p <0.001 by analysis of variance compared with the controls.
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Bioss anti adipophilin
Oleic acid (C18:1)-induced vanin-1 mRNA expression during the course of lipid accumulation in HuH-7 cells. (A) Immunofluorescence to show lipid accumulation (green) and nuclei (blue) in human hepatoma cell line HuH-7. After 24-h induction with 0 (control), 0.01, 0.1, 1, and 2 mM oleic acid, HuH-7 cells were fixed and observed by confocal laser-scanning microscopy. Note the absence of green fluorescence at oleic acid concentrations of 0.01 and 0.1 mM. (B)–(D) Relative expressions of vanin-1 (B), PPARα (C), and <t>ADRP</t> (D) in HuH-7 cells with the same doses of oleic acid. The values shown are the mean (SEM) ( n = 6); *** p <0.001 by analysis of variance compared with the controls.
Anti Adipophilin, supplied by Bioss, 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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ProSci Incorporated control rabbit immunoglobulin
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
Control Rabbit Immunoglobulin, supplied by ProSci Incorporated, 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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Proteintech 1 ap proteintech cd63
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
1 Ap Proteintech Cd63, supplied by Proteintech, 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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Cusabio inflammatory cytokines
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
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Gallus BioPharmaceuticals adipocyte differentiation-related protein
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
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Progen Biotechnik perilipin-2
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
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87
Thermo Fisher gene exp bmp15 hs00193764 m1
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
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Thermo Fisher gene exp vash1 mm00616592 m1
A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit <t>immunoglobulin</t> (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.
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Progen Biotechnik adipophilin
Representative immunohistochemical findings of chromophobe renal cell carcinoma (ChRCC): (A) all ChRCCs were negative for vimentin (case Y2), (B) most ChRCCs showed membranous positivity for c-kit (case Y2), (C) ChRCC typically showed diffuse strong positivity for CK7 (case Y2), and (D) some ChRCCs showed positivity for <t>adipophilin</t> (case Y6).
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Feto Maternal and GenetYX Center il-6 cytokine
Involvement of IL-6 and IL-8 in a healthy pregnancy.
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Thermo Fisher recombinant human adrp protein
( A ) Schematic of the microfluidic system to form a free-standing bilayer containing Proteo-LDs. ( B ) The secondary structure of <t>ADRP</t> was provided by the AlphaFold AI database. ADRP is reconstituted in the PC:PE monolayer covering the LD. ( C ) A bilayer is formed at the aperture between the channel and the cone, and LDs containing <t>ADRP</t> <t>protein</t> are introduced from the bottom channel and insert into the bilayer. ( D ) Schematic of the microfluidic device to form the free-standing monolayer. A phospholipid monolayer is formed at the buffer–triolein interface.
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Image Search Results


Oleic acid (C18:1)-induced vanin-1 mRNA expression during the course of lipid accumulation in HuH-7 cells. (A) Immunofluorescence to show lipid accumulation (green) and nuclei (blue) in human hepatoma cell line HuH-7. After 24-h induction with 0 (control), 0.01, 0.1, 1, and 2 mM oleic acid, HuH-7 cells were fixed and observed by confocal laser-scanning microscopy. Note the absence of green fluorescence at oleic acid concentrations of 0.01 and 0.1 mM. (B)–(D) Relative expressions of vanin-1 (B), PPARα (C), and ADRP (D) in HuH-7 cells with the same doses of oleic acid. The values shown are the mean (SEM) ( n = 6); *** p <0.001 by analysis of variance compared with the controls.

Journal: Journal of Clinical Biochemistry and Nutrition

Article Title: Analysis of vanin-1 upregulation and lipid accumulation in hepatocytes in response to a high-fat diet and free fatty acids

doi: 10.3164/jcbn.12-06

Figure Lengend Snippet: Oleic acid (C18:1)-induced vanin-1 mRNA expression during the course of lipid accumulation in HuH-7 cells. (A) Immunofluorescence to show lipid accumulation (green) and nuclei (blue) in human hepatoma cell line HuH-7. After 24-h induction with 0 (control), 0.01, 0.1, 1, and 2 mM oleic acid, HuH-7 cells were fixed and observed by confocal laser-scanning microscopy. Note the absence of green fluorescence at oleic acid concentrations of 0.01 and 0.1 mM. (B)–(D) Relative expressions of vanin-1 (B), PPARα (C), and ADRP (D) in HuH-7 cells with the same doses of oleic acid. The values shown are the mean (SEM) ( n = 6); *** p <0.001 by analysis of variance compared with the controls.

Article Snippet: TaqMan probes for mouse vanin-1 (Mm00495965_m1), human vanin-1 (Hs00190982_m1), human PPARα (Hs00947539_m1), and human adipose differentiation-related protein (ADRP; Hs00605340_m1) were purchased from Applied Biosystems.

Techniques: Expressing, Immunofluorescence, Control, Confocal Laser Scanning Microscopy, Fluorescence

A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit immunoglobulin (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.

Journal:

Article Title: Expression of RASSF1A, an epigenetically silenced tumor suppressor, overcomes resistance to apoptosis induction by interferons

doi: 10.1158/0008-5472.CAN-05-2303

Figure Lengend Snippet: A): Map of lentiviral RASSF1A construct. B): ACHN cells were transduced with RASSF1A carrying lentivirus or empty virus. 72h later selective antibiotic was added and the population of clones was grown in selection media for 14 days before assessing apoptotic response to IFN-β (50 U/ml over 5 days) by TUNEL assay. After confirmation of stable expression of RASSF1A by immunoblotting, clonal selection was performed to identify clones that expressed similar amounts of RASSF1A protein as achieved by DNMT1 AS (40 nM) over 8 days. Treatment with DNMT1 mismatch control oligonucleotide (MM) and empty lentivirus transduced cells served as negative controls. In clones expressing RASSF1A at levels comparable to DNA demethylating treatment, IFN-β (50 U/ml over 5 days) resulted in 20–40% apoptotic cells while stable transduction with empty lentivirus (kept in selective antibiotic for equal amounts of time) did not. C): Concurrent treatment of ACHN RASSF1A clone 1.3 with 2 μg/ml TRAIL neutralizing antibody (TRAIL-N AB) and IFN-β (50 U/ml) over 5 days inhibited IFN-induced apoptosis compared to cotreatment with 2 μg/ml control rabbit immunoglobulin (CTRL AB). D): RASSF1A expression markedly increased sensitivity to apoptosis induction by Apo2L/TRAIL in ACHN cells. Normal kidney epithelial (NKE) cells, even after pretreatment with 5-AZA-dC (200 nM) over 4 days, which alone resulted in moderate apoptosis induction, remained resistant to the apoptosis inducing effects of Apo2L/TRAIL. TUNEL graphs display the means and standard deviations (error bars) of independent experiments.

Article Snippet: Apo2L / TRAIL was obtained from PeproTech (Rocky Hill, NJ), rabbit polyclonal TRAIL neutralizing antibody and control rabbit immunoglobulin from ProSci (Poway, CA).

Techniques: Construct, Transduction, Virus, Clone Assay, Selection, TUNEL Assay, Expressing, Western Blot, Control

Representative immunohistochemical findings of chromophobe renal cell carcinoma (ChRCC): (A) all ChRCCs were negative for vimentin (case Y2), (B) most ChRCCs showed membranous positivity for c-kit (case Y2), (C) ChRCC typically showed diffuse strong positivity for CK7 (case Y2), and (D) some ChRCCs showed positivity for adipophilin (case Y6).

Journal: Clinical Pathology

Article Title: Clinicopathological and Molecular Characteristics of Macroscopically Yellowish-Colored Chromophobe Renal Cell Carcinoma Compared to Non-Yellowish-Colored Chromophobe Renal Cell Carcinoma

doi: 10.1177/2632010X211064821

Figure Lengend Snippet: Representative immunohistochemical findings of chromophobe renal cell carcinoma (ChRCC): (A) all ChRCCs were negative for vimentin (case Y2), (B) most ChRCCs showed membranous positivity for c-kit (case Y2), (C) ChRCC typically showed diffuse strong positivity for CK7 (case Y2), and (D) some ChRCCs showed positivity for adipophilin (case Y6).

Article Snippet: We used the following primary antibodies: vimentin (V9 mouse monoclonal, Roche, Basel, CH, ready-to-use [RTU], heat, pH9), c-kit (rabbit polyclonal, Dako, Tokyo, Japan, 1:200, heat, pH9), cytokeratin 7 (CK7) (SP52 rabbit monoclonal, Roche, Basel, CH, RTU, heat, pH9), SDHB (21A11AE7 mouse monoclonal, abcam, Tokyo, JPN, 1:400, heat, pH6), chromogranin A (LK2H10 mouse monoclonal, Roche, Basal, CH, RTU, heat, pH9), synaptophysin (MRQ-40 rabbit monoclonal, Roche, Basal, CH, RTU, hear, pH9), INSM-1 (A-8 mouse monoclonal, Santa Cruz Biotechnology, Dallas, TX, USA, 1:100, heat, pH9), and adipophilin (AP125 mouse monoclonal, Progen, Heidelberg, DE, 1:400, heat, pH9).

Techniques: Immunohistochemical staining

Immunohistochemical findings of chromophobe renal cell carcinoma.

Journal: Clinical Pathology

Article Title: Clinicopathological and Molecular Characteristics of Macroscopically Yellowish-Colored Chromophobe Renal Cell Carcinoma Compared to Non-Yellowish-Colored Chromophobe Renal Cell Carcinoma

doi: 10.1177/2632010X211064821

Figure Lengend Snippet: Immunohistochemical findings of chromophobe renal cell carcinoma.

Article Snippet: We used the following primary antibodies: vimentin (V9 mouse monoclonal, Roche, Basel, CH, ready-to-use [RTU], heat, pH9), c-kit (rabbit polyclonal, Dako, Tokyo, Japan, 1:200, heat, pH9), cytokeratin 7 (CK7) (SP52 rabbit monoclonal, Roche, Basel, CH, RTU, heat, pH9), SDHB (21A11AE7 mouse monoclonal, abcam, Tokyo, JPN, 1:400, heat, pH6), chromogranin A (LK2H10 mouse monoclonal, Roche, Basal, CH, RTU, heat, pH9), synaptophysin (MRQ-40 rabbit monoclonal, Roche, Basal, CH, RTU, hear, pH9), INSM-1 (A-8 mouse monoclonal, Santa Cruz Biotechnology, Dallas, TX, USA, 1:100, heat, pH9), and adipophilin (AP125 mouse monoclonal, Progen, Heidelberg, DE, 1:400, heat, pH9).

Techniques: Immunohistochemical staining

Involvement of IL-6 and IL-8 in a healthy pregnancy.

Journal: International Journal of Molecular Sciences

Article Title: IL-6 and IL-8: An Overview of Their Roles in Healthy and Pathological Pregnancies

doi: 10.3390/ijms232314574

Figure Lengend Snippet: Involvement of IL-6 and IL-8 in a healthy pregnancy.

Article Snippet: The general information related to IL-6 and IL-8 functions is followed by an overview of their overall expression in cycling endometrium and at the feto-maternal interface.

Techniques: In Vitro, Migration, Expressing

( A ) Schematic of the microfluidic system to form a free-standing bilayer containing Proteo-LDs. ( B ) The secondary structure of ADRP was provided by the AlphaFold AI database. ADRP is reconstituted in the PC:PE monolayer covering the LD. ( C ) A bilayer is formed at the aperture between the channel and the cone, and LDs containing ADRP protein are introduced from the bottom channel and insert into the bilayer. ( D ) Schematic of the microfluidic device to form the free-standing monolayer. A phospholipid monolayer is formed at the buffer–triolein interface.

Journal: International Journal of Molecular Sciences

Article Title: Bilayer-Embedded Lipid Droplets Coated with Perilipin-2 Display a Pancake Shape

doi: 10.3390/ijms24032072

Figure Lengend Snippet: ( A ) Schematic of the microfluidic system to form a free-standing bilayer containing Proteo-LDs. ( B ) The secondary structure of ADRP was provided by the AlphaFold AI database. ADRP is reconstituted in the PC:PE monolayer covering the LD. ( C ) A bilayer is formed at the aperture between the channel and the cone, and LDs containing ADRP protein are introduced from the bottom channel and insert into the bilayer. ( D ) Schematic of the microfluidic device to form the free-standing monolayer. A phospholipid monolayer is formed at the buffer–triolein interface.

Article Snippet: Prior to conjugation, a stock solution with a concentration of 0.5 mg/mL was prepared by mixing the recombinant human ADRP protein with ultra-pure water (Thermo Fisher, Waltham, MA, USA).

Techniques: