glyceraldehyde 3 phosphate dehydrogenase gapdh Santa Cruz Biotechnology Search Results


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  • 95
    Millipore glyceraldehyde 3 phosphate dehydrogenase gapdh antibody
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh
    PRL inhibits BCL6 expression via miR-339-5p pathways. (A) qRT-PCR analysis of miR-339-5p mRNA in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (B) MCF-7 and T47D cells were grown and transiently transfected with miR-339-5p ASO or scrambled sequence oligonucleotides as negative control and subjected to western blot assays. Forty-eight hours later, cells were treated with or without PRL for 6 hours. (C) Corresponding densitometry data of BCL6 normalized to <t>GAPDH</t> loading controls. (D) qRT-PCR analysis of BCL6 was performed in MCF-7 and T47D cells, respectively. PRL=prolactin; BCL6 =B-cell lymphoma 6; <t>GAPDH=glyceraldehyde-3-phosphate</t> dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction; ASO=antisense oligonucleotide. * p
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    Santa Cruz Biotechnology protein glyceraldehyde 3 phosphate dehydrogenase gapdh
    PRL inhibits BCL6 expression via miR-339-5p pathways. (A) qRT-PCR analysis of miR-339-5p mRNA in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (B) MCF-7 and T47D cells were grown and transiently transfected with miR-339-5p ASO or scrambled sequence oligonucleotides as negative control and subjected to western blot assays. Forty-eight hours later, cells were treated with or without PRL for 6 hours. (C) Corresponding densitometry data of BCL6 normalized to <t>GAPDH</t> loading controls. (D) qRT-PCR analysis of BCL6 was performed in MCF-7 and T47D cells, respectively. PRL=prolactin; BCL6 =B-cell lymphoma 6; <t>GAPDH=glyceraldehyde-3-phosphate</t> dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction; ASO=antisense oligonucleotide. * p
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh fl 335
    Vasculotide treatment reduces vascular inflammation and tissue infiltration in kidney transplantation. Fluorescent immunohistochemistry for (A) ICAM-1 (red), (B) Gr-1 (red) and (C) F4/80 (red) in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; D: Immunoblot of murine kidney homogenate for ICAM-1 and <t>GAPDH</t> for the same conditions. VT: Vasculotide; ICAM-1: Intercellular adhesion molecule; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.
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    Santa Cruz Biotechnology hdac1 glyceraldehyde 3 phosphate dehydrogenase gapdh
    Vasculotide treatment reduces vascular inflammation and tissue infiltration in kidney transplantation. Fluorescent immunohistochemistry for (A) ICAM-1 (red), (B) Gr-1 (red) and (C) F4/80 (red) in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; D: Immunoblot of murine kidney homogenate for ICAM-1 and <t>GAPDH</t> for the same conditions. VT: Vasculotide; ICAM-1: Intercellular adhesion molecule; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.
    Hdac1 Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology located glyceraldehyde 3 phosphate dehydrogenase gapdh enzyme
    Transfection of HEK-293 cells with pCEP4HIF-1α led to expression of the HIF-1α protein Nuclear protein extracts (Nuc) from HEK-293 cells transfected with pCEP4HIF-1α (HIF-1α) yielded a stronger 120 kDa band, the expected size of the HIF-1α protein, on a Western blot probed with a HIF-1α antibody, than nuclear extracts from pAP-lacZ transfected cells (sham). Cytoplasmic protein extracts (Cyt) displayed no band. <t>Glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> and histone H4 were used as loading controls for the cytoplasmic and nuclear protein fractions, respectively.
    Located Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Enzyme, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology gene glyceraldehyde 3 phosphate dehydrogenase gapdh
    Transfection of HEK-293 cells with pCEP4HIF-1α led to expression of the HIF-1α protein Nuclear protein extracts (Nuc) from HEK-293 cells transfected with pCEP4HIF-1α (HIF-1α) yielded a stronger 120 kDa band, the expected size of the HIF-1α protein, on a Western blot probed with a HIF-1α antibody, than nuclear extracts from pAP-lacZ transfected cells (sham). Cytoplasmic protein extracts (Cyt) displayed no band. <t>Glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> and histone H4 were used as loading controls for the cytoplasmic and nuclear protein fractions, respectively.
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology control glyceraldehyde 3 phosphate dehydrogenase gapdh
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh sc 47 724
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology monoclonal glyceraldehyde 3 phosphate dehydrogenase gapdh antibody
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology monoclonal antibody against glyceraldehyde 3 phosphate dehydrogenase gapdh
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase rabbit gapdh pab
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh 6c5
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology glyceraldehydes 3 phosphate dehydrogenase gapdh
    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p
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    Santa Cruz Biotechnology rabbit polyclonal anti glyceraldehyde 3 phosphate dehydrogenase gapdh
    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh antibody antibody sc 365062
    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Santa Cruz Biotechnology human glyceraldehyde 3 phosphate dehydrogenase gapdh
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    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Santa Cruz Biotechnology glycerol glyceraldehyde 3 phosphate dehydrogenase
    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Santa Cruz Biotechnology anti glyceraldehyde 3 phosphate dehydrogenase gapdh sc 25778 1 1000
    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (lower panel). Data are representative of three separate experiments.
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    Santa Cruz Biotechnology goat polyclonal antibody against glyceraldehyde 3 phosphate dehydrogenase gapdh
    Cend1 and RanBPM interact in vitro and form complexes. ( a ) In a cell-free system, a 942 bp fragment corresponding to the SPRY-LISH-CTLH domain of RanBPM was 35 S-labeled during coupled transcription/translation reactions and was then used in GST-pull down assays with GST-Cend1 protein or GST alone as negative control. GST-Cend1 specifically precipitates the SPRY-LISH-CTLH domain of RanBPM (upper panel). GST and GST-Cend1 protein loading is shown in the lower panel. ( b ) Reciprocal GST-pull down assays were performed in solubilized fractions of mouse brain homogenate where Cend1 is expressed in abundance (upper panel, input). GST-RanBPM (981bp) and GST-RanBPM (1731bp) fusion proteins precipitate the native Cend1 protein from mouse brain (middle panel). GST protein loading is shown in the lower panel. Cend1 immunoprecipitation with <t>polyclonal</t> anti-Cend1 antibody served as a positive control. ( c ) HEK 293T cells were transiently transfected with FLAG-tagged RanBPM and GST pull-down assays were performed with GST-Cend1 or GST as negative control (GST protein loading, upper panel). RanBPM (input, middle panel) was specifically precipitated by GST-Cend1 (lower panel). ( d ) Cend1 and RanBPM associate in vivo in HEK 293T cells. HEK293T cells were transiently transfected with Cend1, FLAG-RanBMP or both as indicated. Immunoprecipitation of RanBPM from HEK293T cell lysates was performed using anti-FLAG (upper panel) and detection of co-immunoprecipitated Cend1 was performed by immunoblotting using anti-Cend1 (lower panel). An irrelevant polyclonal antibody against peroxiredoxin II was used for immunoprecipitation, as negative control. ( e ) Cend1 and RanBPM co-localize in the cytoplasm of transiently co-transfected Neuro 2a cells. Double immunofluorescence labeling and confocal microscopy showed that Cend1 (red) is localized in the cytoplasm ( i ), while RanBPM (green) is partitioned in both the cytoplasm and the nucleus as detected by an anti-FLAG antibody (ii). Nuclei (blue) were visualized using TO-PRO-3 (iii) and the merged picture, including orthogonal optical sectioning, is shown in (iv). In (v-viii) shown is staining for the same antigens, but RanBPM is detected by an anti-RanBPM antibody. Scale bar: 10 μm. ( f ) Fractionation analysis of Neuro 2a cells transiently transfected with RanBPM followed by Western blot analysis, confirmed that RanBPM is distributed in both the cytoplasmic (C) and nuclear fractions (N). Fraction purity was checked using <t>anti-GAPDH</t> (cytoplasmic marker) and anti-PH3 (nuclear marker) antibodies, respectively.
    Goat Polyclonal Antibody Against Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology mouse primary antibody against glyceraldehyde 3 phosphate dehydrogenase gapdh
    Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH;</t> 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P
    Mouse Primary Antibody Against Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 82/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology cytoplasmic fractionation control glyceraldehyde 3 phosphate dehydrogenase gapdh
    Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH;</t> 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P
    Cytoplasmic Fractionation Control Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh protein expression
    Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH;</t> 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Protein Expression, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology goat polyclonal glyceraldehyde 3 phosphate dehydrogenase gapdh v 18 antibodies
    Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH;</t> 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P
    Goat Polyclonal Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh V 18 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology glyceraldehydes 3 phosphate dehydrogenase gapdh antibodies
    Western blot analyses of E-cadherin, COX-2 and Snail in colon cancer cells, and morphology of HCT8 transfected with cDNA for COX-2 or Snail. (A and B) Endogenous expressions of E-cadherin, COX-2, and Snail in colon cancer cells, and ectopic expressions of COX-2 and Snail in HCT8 and SW620. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents <t>GAPDH,</t> which was used as a loading control. (C) Ectopic expression of COX-2 or Snail induced a scattered, flattened phenotype with few intercellular contacts in HCT8. COX-2, cyclooxygenase-2; SDS, sodium dodecyl sulfate; cDNA, complementary DNA; GAPDH, glyceraldehydes 3-phosphate dehydrogenase.
    Glyceraldehydes 3 Phosphate Dehydrogenase Gapdh Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    PRL inhibits BCL6 expression via miR-339-5p pathways. (A) qRT-PCR analysis of miR-339-5p mRNA in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (B) MCF-7 and T47D cells were grown and transiently transfected with miR-339-5p ASO or scrambled sequence oligonucleotides as negative control and subjected to western blot assays. Forty-eight hours later, cells were treated with or without PRL for 6 hours. (C) Corresponding densitometry data of BCL6 normalized to GAPDH loading controls. (D) qRT-PCR analysis of BCL6 was performed in MCF-7 and T47D cells, respectively. PRL=prolactin; BCL6 =B-cell lymphoma 6; GAPDH=glyceraldehyde-3-phosphate dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction; ASO=antisense oligonucleotide. * p

    Journal: Journal of Breast Cancer

    Article Title: Prolactin Inhibits BCL6 Expression in Breast Cancer Cells through a MicroRNA-339-5p-Dependent Pathway

    doi: 10.4048/jbc.2016.19.1.26

    Figure Lengend Snippet: PRL inhibits BCL6 expression via miR-339-5p pathways. (A) qRT-PCR analysis of miR-339-5p mRNA in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (B) MCF-7 and T47D cells were grown and transiently transfected with miR-339-5p ASO or scrambled sequence oligonucleotides as negative control and subjected to western blot assays. Forty-eight hours later, cells were treated with or without PRL for 6 hours. (C) Corresponding densitometry data of BCL6 normalized to GAPDH loading controls. (D) qRT-PCR analysis of BCL6 was performed in MCF-7 and T47D cells, respectively. PRL=prolactin; BCL6 =B-cell lymphoma 6; GAPDH=glyceraldehyde-3-phosphate dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction; ASO=antisense oligonucleotide. * p

    Article Snippet: Reagents and antibodies Antibodies against BCL6 and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were obtained from Santa Cruz Biotechnology (Santa Cruz, USA).

    Techniques: Expressing, Quantitative RT-PCR, Transfection, Allele-specific Oligonucleotide, Sequencing, Negative Control, Western Blot, Reverse Transcription Polymerase Chain Reaction

    PRL suppresses BCL6 protein and mRNA levels in breast cancer cells. (A) T47D cells were treated with or without the indicated doses of PRL for 24 hours. Detergent cell extracts were resolved by Western blot. (B) Western blot of representative over time showing protein levels of BCL6 and GAPDH in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (C) Corresponding densitometry data of BCL6 normalized to GAPDH loading controls. (D) Time course of BCL6 mRNA levels in MCF-7 and T47D cells in response to PRL treatment by qRT-PCR. The data are represented as mean±SD from three independent experiments. PRL=prolactin; BCL6 =B-cell lymphoma 6; GAPDH=glyceraldehyde-3-phosphate dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction. * p

    Journal: Journal of Breast Cancer

    Article Title: Prolactin Inhibits BCL6 Expression in Breast Cancer Cells through a MicroRNA-339-5p-Dependent Pathway

    doi: 10.4048/jbc.2016.19.1.26

    Figure Lengend Snippet: PRL suppresses BCL6 protein and mRNA levels in breast cancer cells. (A) T47D cells were treated with or without the indicated doses of PRL for 24 hours. Detergent cell extracts were resolved by Western blot. (B) Western blot of representative over time showing protein levels of BCL6 and GAPDH in MCF-7 and T47D cells treated with or without PRL for up to 48 hours. (C) Corresponding densitometry data of BCL6 normalized to GAPDH loading controls. (D) Time course of BCL6 mRNA levels in MCF-7 and T47D cells in response to PRL treatment by qRT-PCR. The data are represented as mean±SD from three independent experiments. PRL=prolactin; BCL6 =B-cell lymphoma 6; GAPDH=glyceraldehyde-3-phosphate dehydrogenase; qRT-PCR=quantitative reverse transcription-polymerase chain reaction. * p

    Article Snippet: Reagents and antibodies Antibodies against BCL6 and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were obtained from Santa Cruz Biotechnology (Santa Cruz, USA).

    Techniques: Western Blot, Quantitative RT-PCR, Reverse Transcription Polymerase Chain Reaction

    Effects of a combination of rapamycin (RP) and mycophenolic acid (MPA) on tumor necrosis factor (TNF)-α-induced expression of pro-inflammatory genes in HaCaT cells. HaCaT cells were pre-incubated for 24 h and then stimulated with TNF-α (20 ng/ml) after a 1 h pretreatment with RP, MPA, or a combination of the two drugs for 6 h. Pro-inflammatory gene expression was analyzed by reverse transcription-polymerase chain reaction (RT-PCR) using specific primers. The experiment was repeated independently at least three times. IL: interleukin, GAPDH: glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Annals of Dermatology

    Article Title: Synergistic Inhibition of Tumor Necrosis Factor-Alpha-Stimulated Pro-Inflammatory Cytokine Expression in HaCaT Cells by a Combination of Rapamycin and Mycophenolic Acid

    doi: 10.5021/ad.2015.27.1.32

    Figure Lengend Snippet: Effects of a combination of rapamycin (RP) and mycophenolic acid (MPA) on tumor necrosis factor (TNF)-α-induced expression of pro-inflammatory genes in HaCaT cells. HaCaT cells were pre-incubated for 24 h and then stimulated with TNF-α (20 ng/ml) after a 1 h pretreatment with RP, MPA, or a combination of the two drugs for 6 h. Pro-inflammatory gene expression was analyzed by reverse transcription-polymerase chain reaction (RT-PCR) using specific primers. The experiment was repeated independently at least three times. IL: interleukin, GAPDH: glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Antibodies specific to ICAM-1, phospho-extracellular signal-related kinases (ERK), phospho-IκBα, and lamin B were purchased from Cell Signaling Technology (Beverly, MA, USA). phosphor-c-Jun N-terminal kinases (JNK) and Phosphor-p38, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies were purchased from Santa Cruz Biotechnology Inc. (Santa Cruz, CA, USA), and inducible nitric oxide synthase (iNOS) antibodies were obtained from BD Bioscience (San Jose, CA, USA).

    Techniques: Expressing, Incubation, Reverse Transcription Polymerase Chain Reaction

    Melittin attenuates the expression of pro-inflammatory cytokine in obstructed kidneys. ( A ) Immunohistochemical staining shows that melittin inhibits the expressions of tumor necrosis factor (TNF)-α and interleukin (IL)-1β in kidneys at 7 days after unilateral ureteral obstruction (UUO) surgery. Immunohistochemical staining was used to evaluate the extent of pro-inflammatory cytokines, which was subsequently quantified. ( B , C ) Western blot analysis and Reverse transcription-polymerase chain reaction (RT-PCR) results show that melittin suppresses the protein and mRNA expressions of TNF-α and IL-1β in UUO kidneys. Glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) levels were analyzed as an internal control. −: not treated, +: treated. These are representative images from each study group. Magnification: 400×. The results are expressed as means ± SE of three independent determinations. * p

    Journal: Molecules

    Article Title: The Protective Effect of Melittin on Renal Fibrosis in an Animal Model of Unilateral Ureteral Obstruction

    doi: 10.3390/molecules21091137

    Figure Lengend Snippet: Melittin attenuates the expression of pro-inflammatory cytokine in obstructed kidneys. ( A ) Immunohistochemical staining shows that melittin inhibits the expressions of tumor necrosis factor (TNF)-α and interleukin (IL)-1β in kidneys at 7 days after unilateral ureteral obstruction (UUO) surgery. Immunohistochemical staining was used to evaluate the extent of pro-inflammatory cytokines, which was subsequently quantified. ( B , C ) Western blot analysis and Reverse transcription-polymerase chain reaction (RT-PCR) results show that melittin suppresses the protein and mRNA expressions of TNF-α and IL-1β in UUO kidneys. Glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) levels were analyzed as an internal control. −: not treated, +: treated. These are representative images from each study group. Magnification: 400×. The results are expressed as means ± SE of three independent determinations. * p

    Article Snippet: The primary antibodies used in this study were as follows: anti-TNF-α, anti-fibronectin, anti-α-SMA (Abcam), anti-TGF-β1 (R & D Systems), anti-IL-1β, anti-collagen type I, and anti-glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) (Santa Cruz Biotechnology).

    Techniques: Expressing, Immunohistochemistry, Staining, Western Blot, Reverse Transcription Polymerase Chain Reaction

    Cyclic AMP sponge is able to bind cAMP in vitro. (A) NCM460 cell lysates immunoprecipitated (IP) using Sp-2-AEA-cAMPS-Agarose beads (Sp-cAMPS): lanes 1–3: input, 4–6: IP, 4: untransfected, 5: mut -NES-cAMP sponge, 6: NES-cAMP sponge. (B) cAMP competitive assay, HeLa cell lysates, lanes 1–3: input, 4–14: IP, 4–8: untranfected, 9: mut -NES-cAMP sponge, 10–14: NES-cAMP sponge, lanes 8 and 14: beads only. Loading control: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH).

    Journal: PLoS ONE

    Article Title: "cAMP Sponge": A Buffer for Cyclic Adenosine 3?, 5?-Monophosphate

    doi: 10.1371/journal.pone.0007649

    Figure Lengend Snippet: Cyclic AMP sponge is able to bind cAMP in vitro. (A) NCM460 cell lysates immunoprecipitated (IP) using Sp-2-AEA-cAMPS-Agarose beads (Sp-cAMPS): lanes 1–3: input, 4–6: IP, 4: untransfected, 5: mut -NES-cAMP sponge, 6: NES-cAMP sponge. (B) cAMP competitive assay, HeLa cell lysates, lanes 1–3: input, 4–14: IP, 4–8: untranfected, 9: mut -NES-cAMP sponge, 10–14: NES-cAMP sponge, lanes 8 and 14: beads only. Loading control: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH).

    Article Snippet: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (1∶2000; Santa Cruz) was used as a loading control for the total cell lysates and to detect protein contamination for the immunoprecipitated proteins.

    Techniques: In Vitro, Immunoprecipitation

    Effects of IL-10 ( A ) and glucose ( B ) at different concentrations on the protein expression of osteoprotegerin (OPG) and receptor activator of nuclear factor-κB ligand (RANKL) in human periodontal ligament fibroblasts. Panel A , lanes 1-6 : cells treated with interleukin-10 (IL-10) at 0, 1, 10, 25, 50, and 100 ng/mL, respectively. Panel B , lanes 1-6 : cells treated with glucose at 0, 5.5, 10, 20, 30, and 40 mmol/L, respectively. GAPDH: anti-glyceraldehyde-3-phosphate dehydrogenase.

    Journal: Brazilian Journal of Medical and Biological Research

    Article Title: Effects of IL-10 and glucose on expression of OPG and RANKL in human periodontal ligament fibroblasts

    doi: 10.1590/1414-431X20154324

    Figure Lengend Snippet: Effects of IL-10 ( A ) and glucose ( B ) at different concentrations on the protein expression of osteoprotegerin (OPG) and receptor activator of nuclear factor-κB ligand (RANKL) in human periodontal ligament fibroblasts. Panel A , lanes 1-6 : cells treated with interleukin-10 (IL-10) at 0, 1, 10, 25, 50, and 100 ng/mL, respectively. Panel B , lanes 1-6 : cells treated with glucose at 0, 5.5, 10, 20, 30, and 40 mmol/L, respectively. GAPDH: anti-glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: The following specific primary antibodies were used: mouse anti-OPG, anti-RANKL, and anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies (Santa Cruz Biotechnology, USA).

    Techniques: Expressing

    Korean Red Ginseng extract (RGE) suppressed epithelial–mesenchymal transition through the expression of Snail and E-cadherin via the Smad- and mitogen-activated protein kinase signaling pathways. (A) Effects of RGE on morphological changes of transforming growth factor-β1 (TGF-β1)-induced epithelial–mesenchymal transition in HT29 cells. The cells were treated with TGF-β1 (10 ng/mL) and RGE (200–600 μg/mL) for 72 h. (B) The expression of E-cadherin and N-cadherin was detected by immunofluorescence in (C) HT29 cells. The cells were plated in an eight-chambered slide and treated with various concentrations of RGE in the presence or absence of TGF-β1 for 72 h, respectively. (C) and (D) The Smad2/3- and p38/ERK-signaling pathways in TGF-β1-treated HT29 cells. TGF-β1 and RGE (200–600 μg/mL) were treated to cells for 72 h. (C) The phosphorylation of Smad2/3, p38, and ERK, and (D) the protein expressions of Snail and E-cadherin were confirmed by Western blotting. ERK, extracellular signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

    Journal: Journal of Ginseng Research

    Article Title: Effect of Korean Red Ginseng extract on colorectal lung metastasis through inhibiting the epithelial–mesenchymal transition via transforming growth factor-β1/Smad-signaling-mediated Snail/E-cadherin expression

    doi: 10.1016/j.jgr.2017.08.007

    Figure Lengend Snippet: Korean Red Ginseng extract (RGE) suppressed epithelial–mesenchymal transition through the expression of Snail and E-cadherin via the Smad- and mitogen-activated protein kinase signaling pathways. (A) Effects of RGE on morphological changes of transforming growth factor-β1 (TGF-β1)-induced epithelial–mesenchymal transition in HT29 cells. The cells were treated with TGF-β1 (10 ng/mL) and RGE (200–600 μg/mL) for 72 h. (B) The expression of E-cadherin and N-cadherin was detected by immunofluorescence in (C) HT29 cells. The cells were plated in an eight-chambered slide and treated with various concentrations of RGE in the presence or absence of TGF-β1 for 72 h, respectively. (C) and (D) The Smad2/3- and p38/ERK-signaling pathways in TGF-β1-treated HT29 cells. TGF-β1 and RGE (200–600 μg/mL) were treated to cells for 72 h. (C) The phosphorylation of Smad2/3, p38, and ERK, and (D) the protein expressions of Snail and E-cadherin were confirmed by Western blotting. ERK, extracellular signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: The anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody was obtained from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA).

    Techniques: Expressing, Immunofluorescence, Western Blot

    Asparaginyl-tRNA synthetase (AsnRS) and prolyl-tRNA synthetase (ProRS) abundance in control and patients cultured fibroblasts assessed by Western blotting. AsnRS (A) and ProRS (B) protein abundance in controls versus patient. Data are normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) abundance and presented as mean ± SE. Controls n = 3–4, with 1–5 independent repeats each. Patient n = 1, with four independent repeats each.

    Journal: Molecular Genetics & Genomic Medicine

    Article Title: Whole exome sequencing reveals mutations in NARS2 and PARS2, encoding the mitochondrial asparaginyl-tRNA synthetase and prolyl-tRNA synthetase, in patients with Alpers syndrome

    doi: 10.1002/mgg3.115

    Figure Lengend Snippet: Asparaginyl-tRNA synthetase (AsnRS) and prolyl-tRNA synthetase (ProRS) abundance in control and patients cultured fibroblasts assessed by Western blotting. AsnRS (A) and ProRS (B) protein abundance in controls versus patient. Data are normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) abundance and presented as mean ± SE. Controls n = 3–4, with 1–5 independent repeats each. Patient n = 1, with four independent repeats each.

    Article Snippet: Polyclonal rabbit antibodies against asparaginyl-tRNA synthetase and prolyl-tRNA synthetase were purchased from Novus Biologicals (Littleton, CO), while the antibody against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was obtained from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Cell Culture, Western Blot

    Oxidative stress and nitric oxide (NO). (A) Left panel : Top . Representative western blot of nitrotyrosinated proteins (3-NT) of livers from HFD and CD rats (n = 4, in each group). Bottom . Densitometry analysis of 3-NT to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ratio. HFD rats exhibited a higher level of oxidative stress. Right panel : Malondialdehyde (MDA) content in HFD and CD rats (n = 5, in each group). (B) Top . Representative western blot of phosphorylated endothelial NO synthase (p-eNOS) of livers from HFD and CD rats (n = 4, in each group). Bottom . Densitometry analysis of p-eNOS to GAPDH ratio. eNOS activity was decreased in HFD rats. (C) NO bioavailability. GMPc intrahepatic levels were significantly different between CD and HFD rats (n = 4, in each group). Values are mean ± SEM.

    Journal: PLoS ONE

    Article Title: Contribution of Cyclooxygenase End Products and Oxidative Stress to Intrahepatic Endothelial Dysfunction in Early Non-Alcoholic Fatty Liver Disease

    doi: 10.1371/journal.pone.0156650

    Figure Lengend Snippet: Oxidative stress and nitric oxide (NO). (A) Left panel : Top . Representative western blot of nitrotyrosinated proteins (3-NT) of livers from HFD and CD rats (n = 4, in each group). Bottom . Densitometry analysis of 3-NT to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ratio. HFD rats exhibited a higher level of oxidative stress. Right panel : Malondialdehyde (MDA) content in HFD and CD rats (n = 5, in each group). (B) Top . Representative western blot of phosphorylated endothelial NO synthase (p-eNOS) of livers from HFD and CD rats (n = 4, in each group). Bottom . Densitometry analysis of p-eNOS to GAPDH ratio. eNOS activity was decreased in HFD rats. (C) NO bioavailability. GMPc intrahepatic levels were significantly different between CD and HFD rats (n = 4, in each group). Values are mean ± SEM.

    Article Snippet: Blots were probed with either mouse anti-3-nitrotyrosination monoclonal antibody diluted 1:1000 (Sigma; Madrid, Spain) or mouse anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody, diluted 1:1000 (Santa Cruz Biotechnology, Santa Cruz, California, USA).

    Techniques: Western Blot, Multiple Displacement Amplification, Activity Assay

    Knockdown of c-Jun abolished the effect of β-catenin (β-cat) on the expression of osterix (OSX) in human pre-osteoblastic and bone marrow stromal cells. (A) The protein levels of c-Jun and OSX in HS-27A (left panel) and MG-63 (right panel) cells were measurd by western blot analyses in normal control cells (NC, lane 1), cells stably transfected with the empty pcDNA3.1 vector (VC, lane 2), cells stably transduced with scramble control shRNA (SC, lane 3), cells stably transfected with constitutively active (∆N151) β-cat (active β-cat, lane 4), and cells stably transfected with constitutively active (∆N151) β-cat and stably transduced with lentiviral shRNA against c-Jun (active β-cat + cJun-shRNA, lane 5). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blotting was used as a loading control. Density of (B) c-Jun and (C) OSX blots was normalized against that of the GAPDH blot to obtain a relative blot density, respectively. Three independent experiments were performed for each western blot analysis. Data are expressed as the means + SD. (D) The mRNA levels of OSX were measured by RT-qPCR assays in the HS-27A (left panel) and MG-63 (right panel) cells and normalized against those of GAPDH. a P

    Journal: International Journal of Molecular Medicine

    Article Title: β-catenin signaling induces the osteoblastogenic differentiation of human pre-osteoblastic and bone marrow stromal cells mainly through the upregulation of osterix expression

    doi: 10.3892/ijmm.2015.2382

    Figure Lengend Snippet: Knockdown of c-Jun abolished the effect of β-catenin (β-cat) on the expression of osterix (OSX) in human pre-osteoblastic and bone marrow stromal cells. (A) The protein levels of c-Jun and OSX in HS-27A (left panel) and MG-63 (right panel) cells were measurd by western blot analyses in normal control cells (NC, lane 1), cells stably transfected with the empty pcDNA3.1 vector (VC, lane 2), cells stably transduced with scramble control shRNA (SC, lane 3), cells stably transfected with constitutively active (∆N151) β-cat (active β-cat, lane 4), and cells stably transfected with constitutively active (∆N151) β-cat and stably transduced with lentiviral shRNA against c-Jun (active β-cat + cJun-shRNA, lane 5). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blotting was used as a loading control. Density of (B) c-Jun and (C) OSX blots was normalized against that of the GAPDH blot to obtain a relative blot density, respectively. Three independent experiments were performed for each western blot analysis. Data are expressed as the means + SD. (D) The mRNA levels of OSX were measured by RT-qPCR assays in the HS-27A (left panel) and MG-63 (right panel) cells and normalized against those of GAPDH. a P

    Article Snippet: OSX (sc-43984-V), c-Jun (sc-29223-V) and control (sc-108080) shRNA lentiviral particles, and goat poly-clonal anti-β-cat (C-18) (sc-1496) antibody (epitope matched to the carboxyl terminal of human β-cat), rabbit polyclonal anti-OSX (Y-21) (sc-133871) antibody, mouse monoclonal anti-cJun (G-4) (sc-74543) antibody, mouse monoclonal anti-cFos (6-2H-2F) (sc-447) antibody and mouse monoclonal anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (6C5; sc-32233) antibody were all purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Expressing, Western Blot, Stable Transfection, Transfection, Plasmid Preparation, Transduction, shRNA, Quantitative RT-PCR

    Protein levels of β-catenin (β-cat) and osterix (OSX) in human pre-osteoblastic and bone marrow stromal cells. In (A) HS-27A human bone marrow stromal cells and (B) MG-63 human pre-osteoblastic cells, the protein levels of cytoplasmic/soluble β-cat were measured by western blot analyses in normal control cells (NC, lane 1), cells stably transfected with the empty pcDNA3.1 vector (VC, lane 2), cells stably transduced with scramble control shRNA (SC, lane 3), cells stably transfected with constitutively active (∆N151) β-cat (active β-cat, lane 4), cells treated with selective β-cat signaling inhibitor CCT031374 (50 µ M) for 30 h (lane 5), cells stably transfected with constitutively active (∆N151) β-cat and stably transduced with OSX-shRNA (active β-cat + OSX-shRNA, lane 6), and cells stably transfected with OSX and treated with CCT031374 (50 µ M) for 30 h (lane 7). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blotting was used as a loading control. Density of the OSX and the cytoplasmic/soluble β-cat blots was normalized against that of the GAPDH blot to obtain a relative blot density. In cells overexpressing ∆N151/active β-cat, the relative density of ∆N151/active β-cat instead of that of wild-type soluble β-cat was calculated and is shown in the bar graph. Three independent experiments were performed for each western blot analysis. Data are expressed as the means + SD. a P

    Journal: International Journal of Molecular Medicine

    Article Title: β-catenin signaling induces the osteoblastogenic differentiation of human pre-osteoblastic and bone marrow stromal cells mainly through the upregulation of osterix expression

    doi: 10.3892/ijmm.2015.2382

    Figure Lengend Snippet: Protein levels of β-catenin (β-cat) and osterix (OSX) in human pre-osteoblastic and bone marrow stromal cells. In (A) HS-27A human bone marrow stromal cells and (B) MG-63 human pre-osteoblastic cells, the protein levels of cytoplasmic/soluble β-cat were measured by western blot analyses in normal control cells (NC, lane 1), cells stably transfected with the empty pcDNA3.1 vector (VC, lane 2), cells stably transduced with scramble control shRNA (SC, lane 3), cells stably transfected with constitutively active (∆N151) β-cat (active β-cat, lane 4), cells treated with selective β-cat signaling inhibitor CCT031374 (50 µ M) for 30 h (lane 5), cells stably transfected with constitutively active (∆N151) β-cat and stably transduced with OSX-shRNA (active β-cat + OSX-shRNA, lane 6), and cells stably transfected with OSX and treated with CCT031374 (50 µ M) for 30 h (lane 7). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) blotting was used as a loading control. Density of the OSX and the cytoplasmic/soluble β-cat blots was normalized against that of the GAPDH blot to obtain a relative blot density. In cells overexpressing ∆N151/active β-cat, the relative density of ∆N151/active β-cat instead of that of wild-type soluble β-cat was calculated and is shown in the bar graph. Three independent experiments were performed for each western blot analysis. Data are expressed as the means + SD. a P

    Article Snippet: OSX (sc-43984-V), c-Jun (sc-29223-V) and control (sc-108080) shRNA lentiviral particles, and goat poly-clonal anti-β-cat (C-18) (sc-1496) antibody (epitope matched to the carboxyl terminal of human β-cat), rabbit polyclonal anti-OSX (Y-21) (sc-133871) antibody, mouse monoclonal anti-cJun (G-4) (sc-74543) antibody, mouse monoclonal anti-cFos (6-2H-2F) (sc-447) antibody and mouse monoclonal anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (6C5; sc-32233) antibody were all purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Western Blot, Stable Transfection, Transfection, Plasmid Preparation, Transduction, shRNA

    Western blot analysis of selected proteins. HepG2 cells were not treated (mock), treated with 0.3% DMSO or treated with NVP at concentrations ranging from 3.37 μM to 819 μM. On day 7 of treatment cells lysates were prepared which were subjected to SDS-PAGE and western blot analysis to detect the expression of actin, voltage dependent anion channel (VDAC), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), peroxiredoxin-1 (PRDX1), Isocitrate dehydrogenase [NADP] cytoplasmic (IDH1), ATP synthase subunit beta, mitochondrial (ATP5B) and vinculin. The experiment was undertaken independently in triplicate. Protein band intensities were quantitated using the imageJ image analysis program and analyzed by GraphPad Prism 5 program and the expression all proteins was normalized to vinculin. Error bars show S.E.M.

    Journal: Scientific Reports

    Article Title: Nevirapine induced mitochondrial dysfunction in HepG2 cells

    doi: 10.1038/s41598-017-09321-y

    Figure Lengend Snippet: Western blot analysis of selected proteins. HepG2 cells were not treated (mock), treated with 0.3% DMSO or treated with NVP at concentrations ranging from 3.37 μM to 819 μM. On day 7 of treatment cells lysates were prepared which were subjected to SDS-PAGE and western blot analysis to detect the expression of actin, voltage dependent anion channel (VDAC), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), peroxiredoxin-1 (PRDX1), Isocitrate dehydrogenase [NADP] cytoplasmic (IDH1), ATP synthase subunit beta, mitochondrial (ATP5B) and vinculin. The experiment was undertaken independently in triplicate. Protein band intensities were quantitated using the imageJ image analysis program and analyzed by GraphPad Prism 5 program and the expression all proteins was normalized to vinculin. Error bars show S.E.M.

    Article Snippet: The membranes were probed overnight at 4 °C with a 1:3,000 dilution of a goat polyclonal anti actin antibody (sc-1616; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), or a 1:1,000 dilution of a mouse monoclonal anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody (sc-32233; Santa Cruz Biotechnology, Inc.), or a 1:3,000 dilution of a rabbit monoclonal anti-voltage dependent anion channel (VDAC) antibody (4661; Cell Signaling, Danvers, MA), or a 1:50,000 dilution of a goat polyclonal anti- peroxiredoxin 1 (PRDX1) antibody (EB09018; One World Lab, San Diego CA), or a 1:1,000 dilution of a rabbit polyclonal anti- isocitrate dehydrogenase 1 (IDH1) antibody (AP7454c; One World Lab), or a 1:2,000 dilution of a mouse monoclonal anti-mitochondrial ATP synthase subunit beta (ATP5B) antibody (TA500850; One World Lab), or a 1:5,000 dilution of a goat polyclonal anti-vinculin antibody (sc-7649; Santa Cruz Biotechnology, Inc).

    Techniques: Western Blot, SDS Page, Expressing

    Vasculotide treatment reduces vascular inflammation and tissue infiltration in kidney transplantation. Fluorescent immunohistochemistry for (A) ICAM-1 (red), (B) Gr-1 (red) and (C) F4/80 (red) in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; D: Immunoblot of murine kidney homogenate for ICAM-1 and GAPDH for the same conditions. VT: Vasculotide; ICAM-1: Intercellular adhesion molecule; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.

    Journal: World Journal of Transplantation

    Article Title: Pharmacological Tie2 activation in kidney transplantation

    doi: 10.5500/wjt.v6.i3.573

    Figure Lengend Snippet: Vasculotide treatment reduces vascular inflammation and tissue infiltration in kidney transplantation. Fluorescent immunohistochemistry for (A) ICAM-1 (red), (B) Gr-1 (red) and (C) F4/80 (red) in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; D: Immunoblot of murine kidney homogenate for ICAM-1 and GAPDH for the same conditions. VT: Vasculotide; ICAM-1: Intercellular adhesion molecule; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (FL-335) (Santa Cruz, 25778) served as loading control for immunoblots.

    Techniques: Transplantation Assay, Immunohistochemistry, Mouse Assay

    Vasculotide ameliorates fibrogenesis. Fluorescent immunohistochemistry of α-smooth-muscle-actin (red) regarding (A) tubular and (B) glomerular injury in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; C: Sirius red staining for the same conditions (D) Immunoblot of murine kidney homogenates for pSMAD3 in healthy (day 0) and kidney transplanted mice (day 28) upon vehicle or VT treatment. VT: Vasculotide; αSMA: α-smooth-muscle-actin; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.

    Journal: World Journal of Transplantation

    Article Title: Pharmacological Tie2 activation in kidney transplantation

    doi: 10.5500/wjt.v6.i3.573

    Figure Lengend Snippet: Vasculotide ameliorates fibrogenesis. Fluorescent immunohistochemistry of α-smooth-muscle-actin (red) regarding (A) tubular and (B) glomerular injury in kidney cross-sections of transplanted mice (vehicle or VT-treated) on day 28 after transplantation. Autofluorescence is shown in green. Images are exemplary for n = 5/condition; C: Sirius red staining for the same conditions (D) Immunoblot of murine kidney homogenates for pSMAD3 in healthy (day 0) and kidney transplanted mice (day 28) upon vehicle or VT treatment. VT: Vasculotide; αSMA: α-smooth-muscle-actin; GAPDH: Glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (FL-335) (Santa Cruz, 25778) served as loading control for immunoblots.

    Techniques: Immunohistochemistry, Mouse Assay, Transplantation Assay, Staining

    Transfection of HEK-293 cells with pCEP4HIF-1α led to expression of the HIF-1α protein Nuclear protein extracts (Nuc) from HEK-293 cells transfected with pCEP4HIF-1α (HIF-1α) yielded a stronger 120 kDa band, the expected size of the HIF-1α protein, on a Western blot probed with a HIF-1α antibody, than nuclear extracts from pAP-lacZ transfected cells (sham). Cytoplasmic protein extracts (Cyt) displayed no band. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and histone H4 were used as loading controls for the cytoplasmic and nuclear protein fractions, respectively.

    Journal: The Journal of Physiology

    Article Title: Hypoxia inducible factor 1? links fast-patterned muscle activity and fast muscle phenotype in rats

    doi: 10.1113/jphysiol.2010.202762

    Figure Lengend Snippet: Transfection of HEK-293 cells with pCEP4HIF-1α led to expression of the HIF-1α protein Nuclear protein extracts (Nuc) from HEK-293 cells transfected with pCEP4HIF-1α (HIF-1α) yielded a stronger 120 kDa band, the expected size of the HIF-1α protein, on a Western blot probed with a HIF-1α antibody, than nuclear extracts from pAP-lacZ transfected cells (sham). Cytoplasmic protein extracts (Cyt) displayed no band. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and histone H4 were used as loading controls for the cytoplasmic and nuclear protein fractions, respectively.

    Article Snippet: Purity of protein fractions was validated using antibodies against the cytoplasmically located glyceraldehyde-3-phosphate dehydrogenase (GAPDH) enzyme (Sc-20357, Santa Cruz Biotechnology), the nuclear histone H4 (Sc-8658, Santa Cruz Biotechnology) or OCT-4 (3576-100, BioVision, Mountain View, CA, USA), diluted 1:500.

    Techniques: Transfection, Expressing, Western Blot

    Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats.  CTGF  mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ).  A :  CTGF  mRNA levels increased six- and sevenfold at both time points.  B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls.  C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p

    Journal: Molecular Vision

    Article Title: Inhibition of connective tissue growth factor by small interfering ribonucleic acid prevents increase in extracellular matrix molecules in a rodent model of diabetic retinopathy

    doi:

    Figure Lengend Snippet: Connective tissue growth factor (CTGF) expression increased in retina of 8 and 12 week diabetic rats. CTGF mRNA expression in the retinas of non-diabetic and diabetic rats after 8 and 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the housekeeping gene acidic ribosomal phosphoprotein P0 ( ARPP 0 ). A : CTGF mRNA levels increased six- and sevenfold at both time points. B : A representative western blot illustrating CTGF and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression in the retinas of diabetic rats after 8 and 12 weeks of hyperglycemia. Note the increased CTGF protein levels compared to the non-diabetic controls. C : Densitometric analysis of three separate immunoblots indicates a 2.5 and 5.7 fold increase in the CTGF protein after 8 and 12 weeks of hyperglycemia, respectively. (*p

    Article Snippet: Membranes were subsequently stripped with Restore Western Blot Stripping (Thermo Scientific), incubated with antibodies to VEGF (1:1,000; Santa Cruz) and to glyceraldehyde 3-phosphate dehydrogenase (GAPDH; 1:1,000; Santa Cruz) for loading control, and processed for immunodetection as described as above.

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot

    siRNA treatment significantly decreased hyperglycemia-induced increase in connective tissue growth factor (CTGF) mRNA and protein, glial fibrillary acidic protein (GFAP), collagen IVα3 and laminin-β1 gene expression. mRNA expression for  CTGF  and selected genes in the retinas of the diabetic rats after 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the TATA-binding protein ( TBP ).  A : Real-time PCR revealed that 3 days post intravitreal injection,  CTGF  siRNA induced a decrease in  CTGF  (33%),  GFAP  (44%), collagen IVα3 (71%), and laminin β1 (63%) mRNAs. In contrast,  CTGF  siRNA did not affect the level of fibronectin or vascular endothelial growth factor ( VEGF ).  B : Immunoblot analysis of CTGF levels in the retinas following a single intravitreal injection of  CTGF  siRNA or scrambled siRNA into left and right eye, respectively. The concentration of the CTGF protein is lower in eyes injected with  CTGF  siRNA.  C : Densitometric analysis of three independent experiments revealed a 54% decrease in CTGF protein in retinas injected with  CTGF  siRNA compared to retinas injected with a scrambled (non-specific) siRNA. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as loading control.  D : Real-time PCR showed that  CTGF  siRNA had no effect on  CTGF  expression 10 days after injection. (*p

    Journal: Molecular Vision

    Article Title: Inhibition of connective tissue growth factor by small interfering ribonucleic acid prevents increase in extracellular matrix molecules in a rodent model of diabetic retinopathy

    doi:

    Figure Lengend Snippet: siRNA treatment significantly decreased hyperglycemia-induced increase in connective tissue growth factor (CTGF) mRNA and protein, glial fibrillary acidic protein (GFAP), collagen IVα3 and laminin-β1 gene expression. mRNA expression for CTGF and selected genes in the retinas of the diabetic rats after 12 weeks of hyperglycemia were analyzed using real-time PCR and normalized to the TATA-binding protein ( TBP ). A : Real-time PCR revealed that 3 days post intravitreal injection, CTGF siRNA induced a decrease in CTGF (33%), GFAP (44%), collagen IVα3 (71%), and laminin β1 (63%) mRNAs. In contrast, CTGF siRNA did not affect the level of fibronectin or vascular endothelial growth factor ( VEGF ). B : Immunoblot analysis of CTGF levels in the retinas following a single intravitreal injection of CTGF siRNA or scrambled siRNA into left and right eye, respectively. The concentration of the CTGF protein is lower in eyes injected with CTGF siRNA. C : Densitometric analysis of three independent experiments revealed a 54% decrease in CTGF protein in retinas injected with CTGF siRNA compared to retinas injected with a scrambled (non-specific) siRNA. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as loading control. D : Real-time PCR showed that CTGF siRNA had no effect on CTGF expression 10 days after injection. (*p

    Article Snippet: Membranes were subsequently stripped with Restore Western Blot Stripping (Thermo Scientific), incubated with antibodies to VEGF (1:1,000; Santa Cruz) and to glyceraldehyde 3-phosphate dehydrogenase (GAPDH; 1:1,000; Santa Cruz) for loading control, and processed for immunodetection as described as above.

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Binding Assay, Injection, Concentration Assay

    Aurora A expression is upregulated by HPV16 E6. (A) The protein levels of Aurora A were enhanced in cervical cancer tissue. Cervical cancer tissue specimens from 10 patients were analyzed for Aurora A expression by immunohistochemistry. A representative sample of cervical cancer tissue (right panel) and the adjacent normal tissue (left panel) are shown. (B) WB showing expression of Aurora A in the E6-knockdown CaSki cell line and the short hairpin RNA control cell line. The protein level of Aurora A was evidently decreased in the E6-knockdown cells compared with the control cells. (C) HEK293 cells were transfected with the PA3F vector or increasing amounts of PA3F E6. Cells were harvested at 36 h post-transfection, and Aurora A protein levels were assessed by WB. This showed that the Aurora A level was upregulated as the transfection of E6 increased. WB, western blot; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Oncology Letters

    Article Title: HPV16 E6 upregulates Aurora A expression

    doi: 10.3892/ol.2016.4786

    Figure Lengend Snippet: Aurora A expression is upregulated by HPV16 E6. (A) The protein levels of Aurora A were enhanced in cervical cancer tissue. Cervical cancer tissue specimens from 10 patients were analyzed for Aurora A expression by immunohistochemistry. A representative sample of cervical cancer tissue (right panel) and the adjacent normal tissue (left panel) are shown. (B) WB showing expression of Aurora A in the E6-knockdown CaSki cell line and the short hairpin RNA control cell line. The protein level of Aurora A was evidently decreased in the E6-knockdown cells compared with the control cells. (C) HEK293 cells were transfected with the PA3F vector or increasing amounts of PA3F E6. Cells were harvested at 36 h post-transfection, and Aurora A protein levels were assessed by WB. This showed that the Aurora A level was upregulated as the transfection of E6 increased. WB, western blot; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The antibodies used in the present study were the mouse monoclonal anti-FLAG M2 (catalog no. F1804; Sigma-Aldrich), anti-HA (catalog no. H3663; Sigma-Aldrich), anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH; Santa Cruz Biotechnology, Inc., Dallas, TX, USA) and anti-Aurora A (catalog no. 610939; BD Biosciences, San Jose, CA, USA) and anti-HPV16 E6 C1P5 (catalog no. sc460; BD Biosciences) antibodies (at 1:1,000 dilution for western blotting).

    Techniques: Expressing, Immunohistochemistry, Western Blot, shRNA, Transfection, Plasmid Preparation

    Aurora A transcript is enhanced in a E6-dependent manner. (A) RT-PCR showed that Aurora A was decreased at a trancription level in CaSki cells with E6 knockdown. (B) HEK293 cells cotransfected with pGL3-basic or pGL3-Aurora A and either pA3F-E6 or an empty vector were harvested at 24 h post-transfection. The cell lysate were subjected to luciferase reporter assay. The results are expressed as the fold RLU change compared with the RLU of cells transfected with pGL3-basic and vector alone. HPV E16 increased the pGL3-Aurora A level. Data is expressed as the mean ± standard deviation of three independent experiments. The WB results of Flag-tagged E6 and GAPDH are shown in the bottom panel. (C) The reporter assay of pGL3-Aurora A promoter cotransfection with an increasing amount (0, 5, 10, 15 and 20 mg) of Flag-tagged E6. At 24 h post-transfection, the cells were harvested and subjected to luciferase reporter assay. The results are expressed as the fold RLU change compared with cells transfected with pGL3-Aurora A and the empty vector alone. RT-PCR, reverse transcription-polymerase chain reaction; RLU, relative luciferase unit; WB, western blot; mRNA, messenger RNA; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Oncology Letters

    Article Title: HPV16 E6 upregulates Aurora A expression

    doi: 10.3892/ol.2016.4786

    Figure Lengend Snippet: Aurora A transcript is enhanced in a E6-dependent manner. (A) RT-PCR showed that Aurora A was decreased at a trancription level in CaSki cells with E6 knockdown. (B) HEK293 cells cotransfected with pGL3-basic or pGL3-Aurora A and either pA3F-E6 or an empty vector were harvested at 24 h post-transfection. The cell lysate were subjected to luciferase reporter assay. The results are expressed as the fold RLU change compared with the RLU of cells transfected with pGL3-basic and vector alone. HPV E16 increased the pGL3-Aurora A level. Data is expressed as the mean ± standard deviation of three independent experiments. The WB results of Flag-tagged E6 and GAPDH are shown in the bottom panel. (C) The reporter assay of pGL3-Aurora A promoter cotransfection with an increasing amount (0, 5, 10, 15 and 20 mg) of Flag-tagged E6. At 24 h post-transfection, the cells were harvested and subjected to luciferase reporter assay. The results are expressed as the fold RLU change compared with cells transfected with pGL3-Aurora A and the empty vector alone. RT-PCR, reverse transcription-polymerase chain reaction; RLU, relative luciferase unit; WB, western blot; mRNA, messenger RNA; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The antibodies used in the present study were the mouse monoclonal anti-FLAG M2 (catalog no. F1804; Sigma-Aldrich), anti-HA (catalog no. H3663; Sigma-Aldrich), anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH; Santa Cruz Biotechnology, Inc., Dallas, TX, USA) and anti-Aurora A (catalog no. 610939; BD Biosciences, San Jose, CA, USA) and anti-HPV16 E6 C1P5 (catalog no. sc460; BD Biosciences) antibodies (at 1:1,000 dilution for western blotting).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Transfection, Luciferase, Reporter Assay, Standard Deviation, Western Blot, Cotransfection

    Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (lower panel). Data are representative of three separate experiments.

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β-Activated Kinase 1 Is Required for Human FcγRIIIb-Induced Neutrophil Extracellular Trap Formation

    doi: 10.3389/fimmu.2016.00277

    Figure Lengend Snippet: Syk is required for FcγRIIIb-mediated TAK1 activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min in the absence or presence of 50 μM Piceatannol (Pic) or 40 nM iSyk, both selective inhibitors of Syk. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE and then Western blotted for phosphorylated-TAK1 (pTAK1) (upper panel), or for phosphorylated ERK (pERK) (middle panel), and for total glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (lower panel). Data are representative of three separate experiments.

    Article Snippet: Rabbit polyclonal anti-ERK 1 (catalog no. sc-94), rabbit polyclonal anti-phospho-ERK 1/2 (pTyr204) (catalog no. sc-101761), and rabbit polyclonal anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (catalog no. sc-25778) were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Activation Assay, SDS Page, Western Blot

    TAK1 is required for FcγRIIIb-mediated ERK activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min, or by 20 nM phorbol 12-myristate 13-acetate (PMA). Some neutrophils were previously treated with 10 nM LL Z1640-2 (LLZ), a selective inhibitor of TAK1. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE, and then, Western blotted for (A) phosphorylated-TAK1 (pTAK1) (upper panel) and for total glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (lower panel); or for (B) phosphorylated ERK (pERK) and total GAPDH (lower panel). Data are representative of three separate experiments.

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β-Activated Kinase 1 Is Required for Human FcγRIIIb-Induced Neutrophil Extracellular Trap Formation

    doi: 10.3389/fimmu.2016.00277

    Figure Lengend Snippet: TAK1 is required for FcγRIIIb-mediated ERK activation . Human neutrophils were left untreated (---), or were stimulated by cross-linking FcγRIIIb for 15 min, or by 20 nM phorbol 12-myristate 13-acetate (PMA). Some neutrophils were previously treated with 10 nM LL Z1640-2 (LLZ), a selective inhibitor of TAK1. Cell lysates were prepared after stimulation. Proteins were resolved by SDS-PAGE, and then, Western blotted for (A) phosphorylated-TAK1 (pTAK1) (upper panel) and for total glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (lower panel); or for (B) phosphorylated ERK (pERK) and total GAPDH (lower panel). Data are representative of three separate experiments.

    Article Snippet: Rabbit polyclonal anti-ERK 1 (catalog no. sc-94), rabbit polyclonal anti-phospho-ERK 1/2 (pTyr204) (catalog no. sc-101761), and rabbit polyclonal anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (catalog no. sc-25778) were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Activation Assay, SDS Page, Western Blot

    Cend1 and RanBPM interact in vitro and form complexes. ( a ) In a cell-free system, a 942 bp fragment corresponding to the SPRY-LISH-CTLH domain of RanBPM was 35 S-labeled during coupled transcription/translation reactions and was then used in GST-pull down assays with GST-Cend1 protein or GST alone as negative control. GST-Cend1 specifically precipitates the SPRY-LISH-CTLH domain of RanBPM (upper panel). GST and GST-Cend1 protein loading is shown in the lower panel. ( b ) Reciprocal GST-pull down assays were performed in solubilized fractions of mouse brain homogenate where Cend1 is expressed in abundance (upper panel, input). GST-RanBPM (981bp) and GST-RanBPM (1731bp) fusion proteins precipitate the native Cend1 protein from mouse brain (middle panel). GST protein loading is shown in the lower panel. Cend1 immunoprecipitation with polyclonal anti-Cend1 antibody served as a positive control. ( c ) HEK 293T cells were transiently transfected with FLAG-tagged RanBPM and GST pull-down assays were performed with GST-Cend1 or GST as negative control (GST protein loading, upper panel). RanBPM (input, middle panel) was specifically precipitated by GST-Cend1 (lower panel). ( d ) Cend1 and RanBPM associate in vivo in HEK 293T cells. HEK293T cells were transiently transfected with Cend1, FLAG-RanBMP or both as indicated. Immunoprecipitation of RanBPM from HEK293T cell lysates was performed using anti-FLAG (upper panel) and detection of co-immunoprecipitated Cend1 was performed by immunoblotting using anti-Cend1 (lower panel). An irrelevant polyclonal antibody against peroxiredoxin II was used for immunoprecipitation, as negative control. ( e ) Cend1 and RanBPM co-localize in the cytoplasm of transiently co-transfected Neuro 2a cells. Double immunofluorescence labeling and confocal microscopy showed that Cend1 (red) is localized in the cytoplasm ( i ), while RanBPM (green) is partitioned in both the cytoplasm and the nucleus as detected by an anti-FLAG antibody (ii). Nuclei (blue) were visualized using TO-PRO-3 (iii) and the merged picture, including orthogonal optical sectioning, is shown in (iv). In (v-viii) shown is staining for the same antigens, but RanBPM is detected by an anti-RanBPM antibody. Scale bar: 10 μm. ( f ) Fractionation analysis of Neuro 2a cells transiently transfected with RanBPM followed by Western blot analysis, confirmed that RanBPM is distributed in both the cytoplasmic (C) and nuclear fractions (N). Fraction purity was checked using anti-GAPDH (cytoplasmic marker) and anti-PH3 (nuclear marker) antibodies, respectively.

    Journal: PLoS ONE

    Article Title: Functional Interactions between BM88/Cend1, Ran-Binding Protein M and Dyrk1B Kinase Affect Cyclin D1 Levels and Cell Cycle Progression/Exit in Mouse Neuroblastoma Cells

    doi: 10.1371/journal.pone.0082172

    Figure Lengend Snippet: Cend1 and RanBPM interact in vitro and form complexes. ( a ) In a cell-free system, a 942 bp fragment corresponding to the SPRY-LISH-CTLH domain of RanBPM was 35 S-labeled during coupled transcription/translation reactions and was then used in GST-pull down assays with GST-Cend1 protein or GST alone as negative control. GST-Cend1 specifically precipitates the SPRY-LISH-CTLH domain of RanBPM (upper panel). GST and GST-Cend1 protein loading is shown in the lower panel. ( b ) Reciprocal GST-pull down assays were performed in solubilized fractions of mouse brain homogenate where Cend1 is expressed in abundance (upper panel, input). GST-RanBPM (981bp) and GST-RanBPM (1731bp) fusion proteins precipitate the native Cend1 protein from mouse brain (middle panel). GST protein loading is shown in the lower panel. Cend1 immunoprecipitation with polyclonal anti-Cend1 antibody served as a positive control. ( c ) HEK 293T cells were transiently transfected with FLAG-tagged RanBPM and GST pull-down assays were performed with GST-Cend1 or GST as negative control (GST protein loading, upper panel). RanBPM (input, middle panel) was specifically precipitated by GST-Cend1 (lower panel). ( d ) Cend1 and RanBPM associate in vivo in HEK 293T cells. HEK293T cells were transiently transfected with Cend1, FLAG-RanBMP or both as indicated. Immunoprecipitation of RanBPM from HEK293T cell lysates was performed using anti-FLAG (upper panel) and detection of co-immunoprecipitated Cend1 was performed by immunoblotting using anti-Cend1 (lower panel). An irrelevant polyclonal antibody against peroxiredoxin II was used for immunoprecipitation, as negative control. ( e ) Cend1 and RanBPM co-localize in the cytoplasm of transiently co-transfected Neuro 2a cells. Double immunofluorescence labeling and confocal microscopy showed that Cend1 (red) is localized in the cytoplasm ( i ), while RanBPM (green) is partitioned in both the cytoplasm and the nucleus as detected by an anti-FLAG antibody (ii). Nuclei (blue) were visualized using TO-PRO-3 (iii) and the merged picture, including orthogonal optical sectioning, is shown in (iv). In (v-viii) shown is staining for the same antigens, but RanBPM is detected by an anti-RanBPM antibody. Scale bar: 10 μm. ( f ) Fractionation analysis of Neuro 2a cells transiently transfected with RanBPM followed by Western blot analysis, confirmed that RanBPM is distributed in both the cytoplasmic (C) and nuclear fractions (N). Fraction purity was checked using anti-GAPDH (cytoplasmic marker) and anti-PH3 (nuclear marker) antibodies, respectively.

    Article Snippet: Other antibodies also used in this study were rabbit polyclonal antibodies against β-tubulin (sc-9104), α-actin and β-actin (sc-1615), mouse monoclonal antibody against βIII-tubulin (Tuj1; Covance, MMS-435P), mouse monoclonal antibody against green fluorescent protein (GFP) (Invitrogen), rabbit polyclonal against phospho-histone 3 (PH3) (Upstate) and goat polyclonal antibody against Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Santa Cruz, sc-20357).

    Techniques: In Vitro, Labeling, Negative Control, Immunoprecipitation, Positive Control, Transfection, In Vivo, Immunofluorescence, Confocal Microscopy, Staining, Fractionation, Western Blot, Marker

    Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH; 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P

    Journal: Journal of Virology

    Article Title: Development of an Alternative Modified Live Influenza B Virus Vaccine

    doi: 10.1128/JVI.00056-17

    Figure Lengend Snippet: Characterization of the IBV PB1 modifications in vitro . (A) HA tag expression in the IAV and IBV carrying a chimeric PB1 HA protein. MDCK cells were either mock inoculated (PBS) (lane 1) or inoculated with WT RG-B/Bris (lane 2), B/Bris ts (lane 3), B/Bris att (lane 4), or the IAV att control (7attWF10:1malH7) (lane 5). PB1 HA chimeric proteins with a molecular mass of > 80 kDa are shown: IAV PB1 HA is indicated by a black arrowhead (predicted molecular mass, 88.66 kDa), and IBV PB1 HA is indicated by an open arrowhead (predicted molecular mass, 85.35 kDa). The host cellular protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH; 38.5 kDa) is shown as a gel loading control. (B and C) Virus polymerase activity at different temperatures. 293T cells were transfected with plasmids encoding the PB1 (or PB1 att ), PB2, PA, and NP and an IBV vRNA-driven luciferase reporter replicon. In addition, a plasmid encoding the secreted alkaline phosphatase (SEAP) under the control of the cytomegalovirus promoter was cotransfected to normalize variations in transfection efficiency. Relative polymerase activity was calculated as the ratio of luciferase activity to alkaline phosphatase activity at 24 hpt (B) or 48 hpt (C). Plotted data represent means ± standard errors. Two-way ANOVA was performed to calculate P values. **, P

    Article Snippet: The membranes were blocked in 5% molecular-grade nonfat dry milk (NFDM; Bio-Rad, Berkeley, CA) for 2 h at room temperature, followed by incubation with a mouse primary antibody against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Santa Cruz Biotech, Dallas, TX) for 2 h at room temperature or a mouse primary antibody against the HA tag (Cell Signaling Technologies, Danvers, MA) overnight at 4°C.

    Techniques: In Vitro, Expressing, Activity Assay, Transfection, Luciferase, Plasmid Preparation

    Western blot analyses of E-cadherin, COX-2 and Snail in colon cancer cells, and morphology of HCT8 transfected with cDNA for COX-2 or Snail. (A and B) Endogenous expressions of E-cadherin, COX-2, and Snail in colon cancer cells, and ectopic expressions of COX-2 and Snail in HCT8 and SW620. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (C) Ectopic expression of COX-2 or Snail induced a scattered, flattened phenotype with few intercellular contacts in HCT8. COX-2, cyclooxygenase-2; SDS, sodium dodecyl sulfate; cDNA, complementary DNA; GAPDH, glyceraldehydes 3-phosphate dehydrogenase.

    Journal: Yonsei Medical Journal

    Article Title: Cyclooxygenase-2 Expression Is Related to the Epithelial-to-Mesenchymal Transition in Human Colon Cancers

    doi: 10.3349/ymj.2009.50.6.818

    Figure Lengend Snippet: Western blot analyses of E-cadherin, COX-2 and Snail in colon cancer cells, and morphology of HCT8 transfected with cDNA for COX-2 or Snail. (A and B) Endogenous expressions of E-cadherin, COX-2, and Snail in colon cancer cells, and ectopic expressions of COX-2 and Snail in HCT8 and SW620. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (C) Ectopic expression of COX-2 or Snail induced a scattered, flattened phenotype with few intercellular contacts in HCT8. COX-2, cyclooxygenase-2; SDS, sodium dodecyl sulfate; cDNA, complementary DNA; GAPDH, glyceraldehydes 3-phosphate dehydrogenase.

    Article Snippet: Cambridge, UK) and anti-glyceraldehydes 3-phosphate dehydrogenase (GAPDH) (1: 200, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA).

    Techniques: Western Blot, Transfection, Polyacrylamide Gel Electrophoresis, Expressing

    Effects of PMA on the expressions of E-cadherin, COX-2, Snail and 15-PGDH, and cell mobility in HCT8 and HT29. (A) Western blot analyses for E-cadherin, COX-2, Snail and 15-PGDH in the presence of PMA (50 ng/mL) at the indicated times. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (B) Cells were incubated with serum-free medium including PMA (50 ng/mL) and allowed to migrate into the wound area for up to 24 hours at 37℃. Images were acquired immediately, and at 4 hours and 24 hours after wounding. PMA (50 ng/mL) treatment increased cell mobility in HCT8 and HT29. COX-2, cyclooxygenase-2; GAPDH, glyceraldehydes 3-phosphate dehydrogenase; PMA, phorbol 12-myristate 13-acetate; 15-PGDH, 15-hydroxyprostaglandin dehydrogenase.

    Journal: Yonsei Medical Journal

    Article Title: Cyclooxygenase-2 Expression Is Related to the Epithelial-to-Mesenchymal Transition in Human Colon Cancers

    doi: 10.3349/ymj.2009.50.6.818

    Figure Lengend Snippet: Effects of PMA on the expressions of E-cadherin, COX-2, Snail and 15-PGDH, and cell mobility in HCT8 and HT29. (A) Western blot analyses for E-cadherin, COX-2, Snail and 15-PGDH in the presence of PMA (50 ng/mL) at the indicated times. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (B) Cells were incubated with serum-free medium including PMA (50 ng/mL) and allowed to migrate into the wound area for up to 24 hours at 37℃. Images were acquired immediately, and at 4 hours and 24 hours after wounding. PMA (50 ng/mL) treatment increased cell mobility in HCT8 and HT29. COX-2, cyclooxygenase-2; GAPDH, glyceraldehydes 3-phosphate dehydrogenase; PMA, phorbol 12-myristate 13-acetate; 15-PGDH, 15-hydroxyprostaglandin dehydrogenase.

    Article Snippet: Cambridge, UK) and anti-glyceraldehydes 3-phosphate dehydrogenase (GAPDH) (1: 200, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA).

    Techniques: Western Blot, Polyacrylamide Gel Electrophoresis, Incubation

    Effects of PGE 2 on the expressions of E-cadherin and Snail, and cell mobility in HCT8 and HT29. (A) Western blot analyses for E-cadherin and Snail in the presence of PGE 2 at the indicated doses for 24 hours. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (B) Cells were incubated with serum-free medium including with PGE 2 (5 µg/mL) and allowed to migrate into the wound area for up to 24 hours at 37℃. Images were acquired immediately, and at 24 hours after wounding. PGE 2 (5 µg/mL) treatment increased cell mobility in HCT8 and HT29. GAPDH, glyceraldehydes 3-phosphate dehydrogenase; PGE 2 , prostaglandin E 2 . SDS, sodium dodecyl sulfate.

    Journal: Yonsei Medical Journal

    Article Title: Cyclooxygenase-2 Expression Is Related to the Epithelial-to-Mesenchymal Transition in Human Colon Cancers

    doi: 10.3349/ymj.2009.50.6.818

    Figure Lengend Snippet: Effects of PGE 2 on the expressions of E-cadherin and Snail, and cell mobility in HCT8 and HT29. (A) Western blot analyses for E-cadherin and Snail in the presence of PGE 2 at the indicated doses for 24 hours. Forty µg of protein was separated by 10% SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The bottom represents GAPDH, which was used as a loading control. (B) Cells were incubated with serum-free medium including with PGE 2 (5 µg/mL) and allowed to migrate into the wound area for up to 24 hours at 37℃. Images were acquired immediately, and at 24 hours after wounding. PGE 2 (5 µg/mL) treatment increased cell mobility in HCT8 and HT29. GAPDH, glyceraldehydes 3-phosphate dehydrogenase; PGE 2 , prostaglandin E 2 . SDS, sodium dodecyl sulfate.

    Article Snippet: Cambridge, UK) and anti-glyceraldehydes 3-phosphate dehydrogenase (GAPDH) (1: 200, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA).

    Techniques: Western Blot, Polyacrylamide Gel Electrophoresis, Incubation