rabbit anti bax  (Millipore)


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    Name:
    Anti BAX
    Description:
    B cell lymphoma 2 associated X BAX also known as CLECSF10 C type lectin superfamily member 10 is located on human chromosome 19q13 BAX is a proapoptotic protein and is a member of Bcl 2 protein family
    Catalog Number:
    sab2108447
    Price:
    None
    Applications:
    Anti-BAX has been used in Western blotting.
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    Structured Review

    Millipore rabbit anti bax
    Anti BAX
    B cell lymphoma 2 associated X BAX also known as CLECSF10 C type lectin superfamily member 10 is located on human chromosome 19q13 BAX is a proapoptotic protein and is a member of Bcl 2 protein family
    https://www.bioz.com/result/rabbit anti bax/product/Millipore
    Average 95 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    rabbit anti bax - by Bioz Stars, 2020-05
    95/100 stars

    Images

    1) Product Images from "Preparation of coffee oil-algae oil-based nanoemulsions and the study of their inhibition effect on UVA-induced skin damage in mice and melanoma cell growth"

    Article Title: Preparation of coffee oil-algae oil-based nanoemulsions and the study of their inhibition effect on UVA-induced skin damage in mice and melanoma cell growth

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S144705

    Effects of coffee oil-algae oil nanoemulsions on protein expressions of cyclin B, CDK2, cyclin A, and CDK1 ( A ), p53 and p21 ( B ), and Bax, Bcl-2, cytochrome C ( C ). Notes: Control cells are incubated with medium only. Results are presented as mean ± standard deviation of triplicate determinations. Data with different letters (A–C) are significantly different at p
    Figure Legend Snippet: Effects of coffee oil-algae oil nanoemulsions on protein expressions of cyclin B, CDK2, cyclin A, and CDK1 ( A ), p53 and p21 ( B ), and Bax, Bcl-2, cytochrome C ( C ). Notes: Control cells are incubated with medium only. Results are presented as mean ± standard deviation of triplicate determinations. Data with different letters (A–C) are significantly different at p

    Techniques Used: Incubation, Standard Deviation

    2) Product Images from "Sodium vanadate combined with l-ascorbic acid delays disease progression, enhances motor performance, and ameliorates muscle atrophy and weakness in mice with spinal muscular atrophy"

    Article Title: Sodium vanadate combined with l-ascorbic acid delays disease progression, enhances motor performance, and ameliorates muscle atrophy and weakness in mice with spinal muscular atrophy

    Journal: BMC Medicine

    doi: 10.1186/1741-7015-11-38

    L-Ascorbic acid (L-AA) eliminates sodium vanadate (SV)-induced cytotoxicity . (A) Western blots showing survival motor neuron (SMN) expression in SMN2 -NSC34 cells treated with 400 μM L -AA, 200 μM SV, or SV combined with L -AA at different time points. β-Actin was used as an internal control. (B-D) Quantification of SMN protein expression in (A). (E-G) Quantification of the viability of SMN2 -NSC34 cells (E) and human dermal fibroblasts (HDFs) (F, G) treated with L -AA, SV or SV combined with L -AA. (H, I) Western blots showing SMN and B cell lymphoma 2-associated X protein (Bax) expression in SMN2 -NSC34 cells (H) and HDFs (I) treated with vehicle, L -AA, SV or SV combined with L -AA. β-Actin was used as an internal control. (J, K) Quantification of SMN and Bax expression in (H). (L, M) Quantification of SMN and Bax expression in (I). The experiment was repeated at least three times, and the mean ± SEM was calculated. Statistical comparisons were performed by one-way analysis of variance (ANOVA) (E-G) and Student's t test (B-D, and J-M).* P
    Figure Legend Snippet: L-Ascorbic acid (L-AA) eliminates sodium vanadate (SV)-induced cytotoxicity . (A) Western blots showing survival motor neuron (SMN) expression in SMN2 -NSC34 cells treated with 400 μM L -AA, 200 μM SV, or SV combined with L -AA at different time points. β-Actin was used as an internal control. (B-D) Quantification of SMN protein expression in (A). (E-G) Quantification of the viability of SMN2 -NSC34 cells (E) and human dermal fibroblasts (HDFs) (F, G) treated with L -AA, SV or SV combined with L -AA. (H, I) Western blots showing SMN and B cell lymphoma 2-associated X protein (Bax) expression in SMN2 -NSC34 cells (H) and HDFs (I) treated with vehicle, L -AA, SV or SV combined with L -AA. β-Actin was used as an internal control. (J, K) Quantification of SMN and Bax expression in (H). (L, M) Quantification of SMN and Bax expression in (I). The experiment was repeated at least three times, and the mean ± SEM was calculated. Statistical comparisons were performed by one-way analysis of variance (ANOVA) (E-G) and Student's t test (B-D, and J-M).* P

    Techniques Used: Western Blot, Expressing

    3) Product Images from "Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland"

    Article Title: Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland

    Journal: Journal of cell science

    doi:

    Binding partners for Bak and Bcl-w in the mouse mammary gland. (A-C) Equal amounts of tissue extracts from lactating (L9) or apoptotic involuting (I2) mouse mammary gland were precipitated with the indicated reagent and the identity of proteins in the precipitates identified by immunoblotting. In each case samples of lysate were also included on the same gels as positive controls (lysate). (A) Immunoprecipitations were performed with sepharoseconjugated anti-Bak and anti-Bax antibodies or control IgG, and the proteins were separated by SDS-PAGE and transferred to nylon. The blots were probed with antibodies to Bak, Bax and Bcl-w. Note that Bcl-w was not present in Bak immunoprecipitates, but did interact with Bax. No Bcl-w was seen either in whole cell lysates or the Bax immunoprecipitates of the I2 sample. (B) Immunoprecipitations with sepharose-conjugated anti-Bcl-x antibodies were separated by SDS-PAGE, transferred to nylon, and probed with antibodies to Bcl-x or Bak. (C) Tissue extracts were mixed with either GST- or GST-Bcl-w conjugated sepharose beads for 2 hours before centrifugation and separation by SDS-PAGE The gels were transferred to nylon and subjected to immunoblotting using antibodies directed against Bak, Bad and Bax. These data confirm that Bcl-w interacts with Bax but not Bak or Bad in mammary epithelial cells. Note that the I2 lysate contains Bax, which is capable of binding GST-Bcl-w, but the absence of Bcl-w at this developmental stage precludes such an interaction taking place in vivo.
    Figure Legend Snippet: Binding partners for Bak and Bcl-w in the mouse mammary gland. (A-C) Equal amounts of tissue extracts from lactating (L9) or apoptotic involuting (I2) mouse mammary gland were precipitated with the indicated reagent and the identity of proteins in the precipitates identified by immunoblotting. In each case samples of lysate were also included on the same gels as positive controls (lysate). (A) Immunoprecipitations were performed with sepharoseconjugated anti-Bak and anti-Bax antibodies or control IgG, and the proteins were separated by SDS-PAGE and transferred to nylon. The blots were probed with antibodies to Bak, Bax and Bcl-w. Note that Bcl-w was not present in Bak immunoprecipitates, but did interact with Bax. No Bcl-w was seen either in whole cell lysates or the Bax immunoprecipitates of the I2 sample. (B) Immunoprecipitations with sepharose-conjugated anti-Bcl-x antibodies were separated by SDS-PAGE, transferred to nylon, and probed with antibodies to Bcl-x or Bak. (C) Tissue extracts were mixed with either GST- or GST-Bcl-w conjugated sepharose beads for 2 hours before centrifugation and separation by SDS-PAGE The gels were transferred to nylon and subjected to immunoblotting using antibodies directed against Bak, Bad and Bax. These data confirm that Bcl-w interacts with Bax but not Bak or Bad in mammary epithelial cells. Note that the I2 lysate contains Bax, which is capable of binding GST-Bcl-w, but the absence of Bcl-w at this developmental stage precludes such an interaction taking place in vivo.

    Techniques Used: Binding Assay, SDS Page, Centrifugation, In Vivo

    High levels of pro-apoptotic Bcl-2 proteins during involution correlate with apoptosis. (A,B) Total RNA was prepared from mammary gland for northern analysis. (A) 10 μg total RNA was blotted onto nylon membranes and hybridised with 32 P-labelled mouse Bax and Bcl-x cDNA. Analysis of β-casein mRNA confirmed that the samples expressed the expected temporal pattern of milk protein genes and an 18S DNA probe was used to assess equal loading of the gels. (B) The blots were analyzed using storage phosphor imaging plates and a Fujix Bas 2000 bioimaging analyzer. The levels of specific mRNA were plotted after normalizing to the level of 18S rRNA. (C) RT-PCR of the cell death genes Bax , Bak and Bad confirmed the RNA profile of Bax as measured by northern blotting and indicated that expression of Bak and Bad were also regulated during development. A 29S ribonuclear protein ( rps29 ) PCR analysis was included to ensure that equal concentrations of RNA were present in the PCR reactions. C, control with no cDNA in the PCR reaction. The faster migrating band in Bak PCR reactions was cloned and sequenced and found to be unrelated to Bak. (D) Multiple bands observed in the involuting day 2 sample of the PCR reaction for Bax were cloned and sequenced. The centrally migrating band corresponded to the major Bax transcript Baxa , while the faster migrating band corresponded to the transcript for Baxγ , which lacks exon 2. The slower migrating band contained a sequence which was unrelated to Bax . (E,F) Whole tissue lysates were prepared from the developmental samples and subjected to polyacrylamide gel electrophoresis. (E) Coomassie staining showed that the protein samples were equally loaded. Western blotting indicated that β-casein was detected in late pregnancy, lactation and early involution, as expected. (F) Similar blots were incubated with antibodies directed against Bax, Bak and Bad. Confirmation of the Bax expression profile was validated using a second independently derived antibody directed against Bax (data not shown). An equal amount of protein from M1 murine myeloid leukaemia cells was included as a positive control for identification of the Bax protein. In each case, and in the subsequent figures, tissue was isolated from 4, 6, or 8 week virgin (v) mice, and at the indicated number of days of pregnancy (P), lactation (L) and involution (I).
    Figure Legend Snippet: High levels of pro-apoptotic Bcl-2 proteins during involution correlate with apoptosis. (A,B) Total RNA was prepared from mammary gland for northern analysis. (A) 10 μg total RNA was blotted onto nylon membranes and hybridised with 32 P-labelled mouse Bax and Bcl-x cDNA. Analysis of β-casein mRNA confirmed that the samples expressed the expected temporal pattern of milk protein genes and an 18S DNA probe was used to assess equal loading of the gels. (B) The blots were analyzed using storage phosphor imaging plates and a Fujix Bas 2000 bioimaging analyzer. The levels of specific mRNA were plotted after normalizing to the level of 18S rRNA. (C) RT-PCR of the cell death genes Bax , Bak and Bad confirmed the RNA profile of Bax as measured by northern blotting and indicated that expression of Bak and Bad were also regulated during development. A 29S ribonuclear protein ( rps29 ) PCR analysis was included to ensure that equal concentrations of RNA were present in the PCR reactions. C, control with no cDNA in the PCR reaction. The faster migrating band in Bak PCR reactions was cloned and sequenced and found to be unrelated to Bak. (D) Multiple bands observed in the involuting day 2 sample of the PCR reaction for Bax were cloned and sequenced. The centrally migrating band corresponded to the major Bax transcript Baxa , while the faster migrating band corresponded to the transcript for Baxγ , which lacks exon 2. The slower migrating band contained a sequence which was unrelated to Bax . (E,F) Whole tissue lysates were prepared from the developmental samples and subjected to polyacrylamide gel electrophoresis. (E) Coomassie staining showed that the protein samples were equally loaded. Western blotting indicated that β-casein was detected in late pregnancy, lactation and early involution, as expected. (F) Similar blots were incubated with antibodies directed against Bax, Bak and Bad. Confirmation of the Bax expression profile was validated using a second independently derived antibody directed against Bax (data not shown). An equal amount of protein from M1 murine myeloid leukaemia cells was included as a positive control for identification of the Bax protein. In each case, and in the subsequent figures, tissue was isolated from 4, 6, or 8 week virgin (v) mice, and at the indicated number of days of pregnancy (P), lactation (L) and involution (I).

    Techniques Used: Northern Blot, Imaging, Reverse Transcription Polymerase Chain Reaction, Expressing, Polymerase Chain Reaction, Clone Assay, Sequencing, Polyacrylamide Gel Electrophoresis, Staining, Western Blot, Incubation, Derivative Assay, Positive Control, Isolation, Mouse Assay

    Schematic representation of changes in the expression profiles of Bcl-2 family proteins during mammary development in the pregnancy cycle. Pro-apoptotic proteins are shown in triangles, while death-suppressors are in circles. More triangles/circles indicate a higher level of expression. Note that (1) Bcl-2 expression is absent in lactation and during the time of maximal apoptosis; (2) the death-promoting molecules Bak and Bad are upregulated at the pregnancy/lactation interface and are proposed to prime the gland for apoptosis, while the survival-promoting molecules Bcl-w and Bcl-x maintain mammary gland integrity during lactation; and (3) Bcl-w is downregulated in involution and may therefore allow apoptosis through the action of Bax, Bak and Bad.
    Figure Legend Snippet: Schematic representation of changes in the expression profiles of Bcl-2 family proteins during mammary development in the pregnancy cycle. Pro-apoptotic proteins are shown in triangles, while death-suppressors are in circles. More triangles/circles indicate a higher level of expression. Note that (1) Bcl-2 expression is absent in lactation and during the time of maximal apoptosis; (2) the death-promoting molecules Bak and Bad are upregulated at the pregnancy/lactation interface and are proposed to prime the gland for apoptosis, while the survival-promoting molecules Bcl-w and Bcl-x maintain mammary gland integrity during lactation; and (3) Bcl-w is downregulated in involution and may therefore allow apoptosis through the action of Bax, Bak and Bad.

    Techniques Used: Expressing

    ). Equivalent amounts of cell protein were separated by polyacrylamide gel electrophoresis, then analyzed by western immunoblotting. Blots were incubated with antibodies directed against Bax, Bak, Bad, Bcl-x, Bcl-2, Bcl-w and β-casein, and lysates from M1 cells are included as controls.
    Figure Legend Snippet: ). Equivalent amounts of cell protein were separated by polyacrylamide gel electrophoresis, then analyzed by western immunoblotting. Blots were incubated with antibodies directed against Bax, Bak, Bad, Bcl-x, Bcl-2, Bcl-w and β-casein, and lysates from M1 cells are included as controls.

    Techniques Used: Polyacrylamide Gel Electrophoresis, Western Blot, Incubation

    4) Product Images from "Targeting redox homeostasis in rhabdomyosarcoma cells: GSH-depleting agents enhance auranofin-induced cell death"

    Article Title: Targeting redox homeostasis in rhabdomyosarcoma cells: GSH-depleting agents enhance auranofin-induced cell death

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2017.412

    Scheme of AUR/BSO- or AUR/ERA-triggered synergistic cell death. AUR inhibits TrxR, which leads to upregulation of GSH, inhibiting AUR. ERA or BSO cause depletion of GSH levels, thereby counteracting the AUR-mediated upregulation of GSH and increasing AUR's cytotoxic activity. This leads to proteasome inhibition and subsequently to accumulation of ubiquitinated NOXA and MCL-1, followed by activation of BAX/BAK and caspases. See text for more details
    Figure Legend Snippet: Scheme of AUR/BSO- or AUR/ERA-triggered synergistic cell death. AUR inhibits TrxR, which leads to upregulation of GSH, inhibiting AUR. ERA or BSO cause depletion of GSH levels, thereby counteracting the AUR-mediated upregulation of GSH and increasing AUR's cytotoxic activity. This leads to proteasome inhibition and subsequently to accumulation of ubiquitinated NOXA and MCL-1, followed by activation of BAX/BAK and caspases. See text for more details

    Techniques Used: Activity Assay, Inhibition, Activation Assay

    5) Product Images from "Human Cytomegalovirus Inhibits Apoptosis by Proteasome-Mediated Degradation of Bax at Endoplasmic Reticulum-Mitochondrion Contacts"

    Article Title: Human Cytomegalovirus Inhibits Apoptosis by Proteasome-Mediated Degradation of Bax at Endoplasmic Reticulum-Mitochondrion Contacts

    Journal: Journal of Virology

    doi: 10.1128/JVI.00145-13

    (A) vMIA recruits Bax to the MAM and mitochondria during HCMV infection. HFFs were uninfected (left) or infected with HCMV wt (BAD wt ; middle) or the HCMV ΔUL37x1 Mut (BAD sub UL37x1; right) at an MOI of 1 PFU/cell. Subcellular fractions were isolated
    Figure Legend Snippet: (A) vMIA recruits Bax to the MAM and mitochondria during HCMV infection. HFFs were uninfected (left) or infected with HCMV wt (BAD wt ; middle) or the HCMV ΔUL37x1 Mut (BAD sub UL37x1; right) at an MOI of 1 PFU/cell. Subcellular fractions were isolated

    Techniques Used: Infection, Isolation

    6) Product Images from "Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli"

    Article Title: Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli

    Journal: EMBO Molecular Medicine

    doi: 10.1002/emmm.201000102

    Increased cytochrome c release and susceptibility to apoptosis in HD A-C. Lymphoblasts of the indicated genotype were treated with 2 µM staurosporine. At the indicated times, viability was determined cytofluorimetrically. Data represent mean ± SE of seven independent experiments. D. Cells of the indicated genotype were treated with 2 µM staurosporine. At the indicated times, cells were lysed and equal amounts of proteins (30 µg) were separated by SDS–PAGE and immunoblotted using the indicated antibodies. E. Densitometric analysis of uncleaved/cleaved PARP levels. Experiments were performed as in (D). Data are normalized to the ratio in untreated samples and represent mean ± SE of four independent experiments. F,H. Mitochondria isolated from lymphoblasts (F) and neurons (H) of the indicated genotype treated where indicated with 2 µM staurosporine for 4 h were treated with BMH where indicated. Equal amounts (40 µg) of mitochondrial protein were analysed by SDS–PAGE/immunoblotting using an anti-BAX antibody. Asterisks: BAX multimers. G. Mitochondria isolated from lymphoblasts of the indicated genotype were treated with cBID for the indicated time and with BMH where indicated. Equal amounts (40 µg) of mitochondrial protein were analysed by SDS–PAGE/immunoblotting using an anti-BAK antibody. Asterisks: BAK multimers. I. Mitochondria isolated from cells of the indicated genotype treated where indicated with 2 µM staurosporine for 4 h were incubated with BMH where indicated. Equal amounts (40 µg) of protein were analysed by SDS–PAGE/immunoblotting using an anti-BAK antibody. Asterisks: BAK multimers. In (F–I) immunoblots are representative of three independent experiments. J. Representative confocal images of striatal cells of the indicated genotype transfected with mtRFP and immunostained with anti-cytochrome c (green) antibody. When indicated, cells were treated for 2 h with 1 mM H 2 O 2 . K. Localization index of cytochrome c . Cells of the indicated genotype were treated where indicated for 2 h with 1 mM H 2 O 2 or for 5 h with 0.75 µM staurosporine (STS). Localization index of cytochrome c was determined as described. Data represent mean ± SE of three independent experiments ( n = 50 cells per condition in each experiment). L-N. Mitochondria isolated from lymphoblasts of the indicated genotype were treated for the indicated times with cBID. The amount of cytochrome c in supernatant and pellet was determined as described. Data represent mean ± SE of four independent experiments. O. Mitochondria from lymphoblasts of the indicated genotype were treated with cBID for the indicated times and then crosslinked with EDC. Equal amounts of proteins were analysed by SDS–PAGE/immunoblotting using anti-OPA1 antibody.
    Figure Legend Snippet: Increased cytochrome c release and susceptibility to apoptosis in HD A-C. Lymphoblasts of the indicated genotype were treated with 2 µM staurosporine. At the indicated times, viability was determined cytofluorimetrically. Data represent mean ± SE of seven independent experiments. D. Cells of the indicated genotype were treated with 2 µM staurosporine. At the indicated times, cells were lysed and equal amounts of proteins (30 µg) were separated by SDS–PAGE and immunoblotted using the indicated antibodies. E. Densitometric analysis of uncleaved/cleaved PARP levels. Experiments were performed as in (D). Data are normalized to the ratio in untreated samples and represent mean ± SE of four independent experiments. F,H. Mitochondria isolated from lymphoblasts (F) and neurons (H) of the indicated genotype treated where indicated with 2 µM staurosporine for 4 h were treated with BMH where indicated. Equal amounts (40 µg) of mitochondrial protein were analysed by SDS–PAGE/immunoblotting using an anti-BAX antibody. Asterisks: BAX multimers. G. Mitochondria isolated from lymphoblasts of the indicated genotype were treated with cBID for the indicated time and with BMH where indicated. Equal amounts (40 µg) of mitochondrial protein were analysed by SDS–PAGE/immunoblotting using an anti-BAK antibody. Asterisks: BAK multimers. I. Mitochondria isolated from cells of the indicated genotype treated where indicated with 2 µM staurosporine for 4 h were incubated with BMH where indicated. Equal amounts (40 µg) of protein were analysed by SDS–PAGE/immunoblotting using an anti-BAK antibody. Asterisks: BAK multimers. In (F–I) immunoblots are representative of three independent experiments. J. Representative confocal images of striatal cells of the indicated genotype transfected with mtRFP and immunostained with anti-cytochrome c (green) antibody. When indicated, cells were treated for 2 h with 1 mM H 2 O 2 . K. Localization index of cytochrome c . Cells of the indicated genotype were treated where indicated for 2 h with 1 mM H 2 O 2 or for 5 h with 0.75 µM staurosporine (STS). Localization index of cytochrome c was determined as described. Data represent mean ± SE of three independent experiments ( n = 50 cells per condition in each experiment). L-N. Mitochondria isolated from lymphoblasts of the indicated genotype were treated for the indicated times with cBID. The amount of cytochrome c in supernatant and pellet was determined as described. Data represent mean ± SE of four independent experiments. O. Mitochondria from lymphoblasts of the indicated genotype were treated with cBID for the indicated times and then crosslinked with EDC. Equal amounts of proteins were analysed by SDS–PAGE/immunoblotting using anti-OPA1 antibody.

    Techniques Used: SDS Page, Isolation, Incubation, Western Blot, Transfection

    7) Product Images from "Anti-Tumor Effects of Bak-Proteoliposomes against Glioblastoma"

    Article Title: Anti-Tumor Effects of Bak-Proteoliposomes against Glioblastoma

    Journal: Molecules

    doi: 10.3390/molecules200915893

    Western Blotting analysis reveals the molecular signaling activated on glioblastoma cells by LB treatment. GL26 cells were treated as described in M M and lysate at different time points. Proteins (50 µg/lane) were separated in SDS-polyacrylamide gels and transferred to nitrocellulose membranes before incubation with antibodies anti-JNKs, pERK, Bax and Mcl-1. Tubulin antibody was used as internal control for loading. Ctrl: untreated cells; LB: Bak Liposomes; BZM: Bortezomib; Eto: Etoposide; Stauro: Staurosporine. Panels ( A – C ): total proteins; panel ( D ): cytoplasmic fraction; and panel ( E ): mitochondrial fraction. Histograms represent the band intensity values; BZM and Stauro treatments are considered as protein-induction positive controls for JNKs and Bax proteins, respectively. Bands analysis was performed using the free software “gel analyzer”. A representative histogram from one out of three experiments (with similar results obtained) is shown.
    Figure Legend Snippet: Western Blotting analysis reveals the molecular signaling activated on glioblastoma cells by LB treatment. GL26 cells were treated as described in M M and lysate at different time points. Proteins (50 µg/lane) were separated in SDS-polyacrylamide gels and transferred to nitrocellulose membranes before incubation with antibodies anti-JNKs, pERK, Bax and Mcl-1. Tubulin antibody was used as internal control for loading. Ctrl: untreated cells; LB: Bak Liposomes; BZM: Bortezomib; Eto: Etoposide; Stauro: Staurosporine. Panels ( A – C ): total proteins; panel ( D ): cytoplasmic fraction; and panel ( E ): mitochondrial fraction. Histograms represent the band intensity values; BZM and Stauro treatments are considered as protein-induction positive controls for JNKs and Bax proteins, respectively. Bands analysis was performed using the free software “gel analyzer”. A representative histogram from one out of three experiments (with similar results obtained) is shown.

    Techniques Used: Western Blot, Incubation, Software

    8) Product Images from "Zinc Chelation Mediates the Lysosomal Disruption without Intracellular ROS Generation"

    Article Title: Zinc Chelation Mediates the Lysosomal Disruption without Intracellular ROS Generation

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2016/6724585

    Influence of the TPEN chelator in the expression levels of apoptotic proteins. SH-SY5Y cells were treated with 25 μ M TPEN. At each time point, 100 μ g of total proteins from the total cell lysates was loaded onto each lane for the detection of p-p38 (a), Bax (b), Bcl-2 (c), JNK (d), and p-JNK (e). β -actin and α -tubulin were used as a loading control. The Western blot images represent three independent experiments, and significant differences between untreated and treated cells were ∗ p
    Figure Legend Snippet: Influence of the TPEN chelator in the expression levels of apoptotic proteins. SH-SY5Y cells were treated with 25 μ M TPEN. At each time point, 100 μ g of total proteins from the total cell lysates was loaded onto each lane for the detection of p-p38 (a), Bax (b), Bcl-2 (c), JNK (d), and p-JNK (e). β -actin and α -tubulin were used as a loading control. The Western blot images represent three independent experiments, and significant differences between untreated and treated cells were ∗ p

    Techniques Used: Expressing, Western Blot

    Related Articles

    MTT Assay:

    Article Title: The effects and mechanism of peiminine-induced apoptosis in human hepatocellular carcinoma HepG2 cells
    Article Snippet: .. RPMI-1640 medium, 3-[4,5-Dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT), propidium iodide (PI), 4,6-diamidino-2-phenylindile(DAPI), dimethyl sulfoxide (DMSO), and anti-Bax, Bcl-2, procaspase-3, -8, -9, caspase-3, -8, -9, PARP1 (Asp214, 89 kD), PARP1 (Asp214, 89 kD) cleaved and β-actin primary antibodies were from Sigma-Aldrich Chemical Co., Ltd (Shanghai, China). ..

    Protein Extraction:

    Article Title: Recombinant VP1, an Akt Inhibitor, Suppresses Progression of Hepatocellular Carcinoma by Inducing Apoptosis and Modulation of CCL2 Production
    Article Snippet: .. Immunoprecipitation For detection of Ku70-Bax interactions in BNL and Hepa1-6 cells, cells treated with or without rVP1 were harvested in protein extraction reagents (Pierce), and 0.2–1 mg of cell lysates were immunoprecipitated with 4–10 µg of anti-Bax antibody (Sigma). .. The immunocomplexes were captured using an immunoprecipitation matrix (ExactaCruz C, Santa Cruz Biotechnology) following the manufacturer's protocol.

    other:

    Article Title: BAD sensitizes breast cancer cells to docetaxel with increased mitotic arrest and necroptosis
    Article Snippet: BAD, tubulin and BAX conformational antibody clone 6A7 were from Sigma-Aldrich.

    TCA Precipitation:

    Article Title: Mitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation
    Article Snippet: .. 400 µl aliquots of each 1 ml collected fraction were concentrated by 20% TCA precipitation, and immunoblotted using anti-Bax, anti-Bak and anti-VDAC antibodies. ..

    Immunoprecipitation:

    Article Title: Recombinant VP1, an Akt Inhibitor, Suppresses Progression of Hepatocellular Carcinoma by Inducing Apoptosis and Modulation of CCL2 Production
    Article Snippet: .. Immunoprecipitation For detection of Ku70-Bax interactions in BNL and Hepa1-6 cells, cells treated with or without rVP1 were harvested in protein extraction reagents (Pierce), and 0.2–1 mg of cell lysates were immunoprecipitated with 4–10 µg of anti-Bax antibody (Sigma). .. The immunocomplexes were captured using an immunoprecipitation matrix (ExactaCruz C, Santa Cruz Biotechnology) following the manufacturer's protocol.

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    Millipore rabbit anti bax
    Effects of coffee oil-algae oil nanoemulsions on protein expressions of <t>cyclin</t> B, CDK2, cyclin A, and CDK1 ( A ), p53 and p21 ( B ), and <t>Bax,</t> Bcl-2, cytochrome C ( C ). Notes: Control cells are incubated with medium only. Results are presented as mean ± standard deviation of triplicate determinations. Data with different letters (A–C) are significantly different at p
    Rabbit Anti Bax, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Effects of coffee oil-algae oil nanoemulsions on protein expressions of cyclin B, CDK2, cyclin A, and CDK1 ( A ), p53 and p21 ( B ), and Bax, Bcl-2, cytochrome C ( C ). Notes: Control cells are incubated with medium only. Results are presented as mean ± standard deviation of triplicate determinations. Data with different letters (A–C) are significantly different at p

    Journal: International Journal of Nanomedicine

    Article Title: Preparation of coffee oil-algae oil-based nanoemulsions and the study of their inhibition effect on UVA-induced skin damage in mice and melanoma cell growth

    doi: 10.2147/IJN.S144705

    Figure Lengend Snippet: Effects of coffee oil-algae oil nanoemulsions on protein expressions of cyclin B, CDK2, cyclin A, and CDK1 ( A ), p53 and p21 ( B ), and Bax, Bcl-2, cytochrome C ( C ). Notes: Control cells are incubated with medium only. Results are presented as mean ± standard deviation of triplicate determinations. Data with different letters (A–C) are significantly different at p

    Article Snippet: The primary antibodies include mouse monoclonal anti-α-tubulin antibody (Sigma–Aldrich Co.), mouse anti-cyclin A and rabbit anti-Bax (EMD Millipore), mouse anti-CDK2, mouse anti-cytochrome C, mouse anti-p21, mouse anti-cyclin B, and mouse anti-Bcl-2 (BD Biosciences), as well as anti-cdc2 (CDK1) and mouse anti-p53 (Novus Biologicals Co., Littleton, CO, USA).

    Techniques: Incubation, Standard Deviation

    Involvement of FLIP and p53 signaling pathways in the regulation of apoptosis in avian H9N2–infected HBE1 and TBE cells. Cytosolic ( C ) and nuclear ( N ) fractions of cell lysates were prepared from uninfected and infected cells at 12 hours ( A and B ) after infection or as indicated, and fractionated on 12–15% SDS-PAGE. Proteins were transferred to PDVF membranes before they were blotted with specific antibodies. Each analysis was performed at least three times, and a representative result is presented. ( A ) FLIP was downregulated in infected cells. ( B ) Bcl-2 family members Bax and Bcl-x s were upregulated in infected cells. ( C ) p53 was phosphorylated at serine 392 in H9N2-infected cells. Arrows indicate phosphorylated p53 bands. *Nonspecific bands, shown in both infected and noninfected cells by the antibody.

    Journal: American Journal of Respiratory Cell and Molecular Biology

    Article Title: Host Immune and Apoptotic Responses to Avian Influenza Virus H9N2 in Human Tracheobronchial Epithelial Cells

    doi: 10.1165/rcmb.2009-0120OC

    Figure Lengend Snippet: Involvement of FLIP and p53 signaling pathways in the regulation of apoptosis in avian H9N2–infected HBE1 and TBE cells. Cytosolic ( C ) and nuclear ( N ) fractions of cell lysates were prepared from uninfected and infected cells at 12 hours ( A and B ) after infection or as indicated, and fractionated on 12–15% SDS-PAGE. Proteins were transferred to PDVF membranes before they were blotted with specific antibodies. Each analysis was performed at least three times, and a representative result is presented. ( A ) FLIP was downregulated in infected cells. ( B ) Bcl-2 family members Bax and Bcl-x s were upregulated in infected cells. ( C ) p53 was phosphorylated at serine 392 in H9N2-infected cells. Arrows indicate phosphorylated p53 bands. *Nonspecific bands, shown in both infected and noninfected cells by the antibody.

    Article Snippet: Anti-Bax rabbit (Ab-1), anti-Bcl-xs rabbit (Ab-1), and anti-Bak monoclonal (Ab-1) antibodies were purchased from EMD Biosciences (Gibbstown, NJ).

    Techniques: Infection, SDS Page

    L-Ascorbic acid (L-AA) eliminates sodium vanadate (SV)-induced cytotoxicity . (A) Western blots showing survival motor neuron (SMN) expression in SMN2 -NSC34 cells treated with 400 μM L -AA, 200 μM SV, or SV combined with L -AA at different time points. β-Actin was used as an internal control. (B-D) Quantification of SMN protein expression in (A). (E-G) Quantification of the viability of SMN2 -NSC34 cells (E) and human dermal fibroblasts (HDFs) (F, G) treated with L -AA, SV or SV combined with L -AA. (H, I) Western blots showing SMN and B cell lymphoma 2-associated X protein (Bax) expression in SMN2 -NSC34 cells (H) and HDFs (I) treated with vehicle, L -AA, SV or SV combined with L -AA. β-Actin was used as an internal control. (J, K) Quantification of SMN and Bax expression in (H). (L, M) Quantification of SMN and Bax expression in (I). The experiment was repeated at least three times, and the mean ± SEM was calculated. Statistical comparisons were performed by one-way analysis of variance (ANOVA) (E-G) and Student's t test (B-D, and J-M).* P

    Journal: BMC Medicine

    Article Title: Sodium vanadate combined with l-ascorbic acid delays disease progression, enhances motor performance, and ameliorates muscle atrophy and weakness in mice with spinal muscular atrophy

    doi: 10.1186/1741-7015-11-38

    Figure Lengend Snippet: L-Ascorbic acid (L-AA) eliminates sodium vanadate (SV)-induced cytotoxicity . (A) Western blots showing survival motor neuron (SMN) expression in SMN2 -NSC34 cells treated with 400 μM L -AA, 200 μM SV, or SV combined with L -AA at different time points. β-Actin was used as an internal control. (B-D) Quantification of SMN protein expression in (A). (E-G) Quantification of the viability of SMN2 -NSC34 cells (E) and human dermal fibroblasts (HDFs) (F, G) treated with L -AA, SV or SV combined with L -AA. (H, I) Western blots showing SMN and B cell lymphoma 2-associated X protein (Bax) expression in SMN2 -NSC34 cells (H) and HDFs (I) treated with vehicle, L -AA, SV or SV combined with L -AA. β-Actin was used as an internal control. (J, K) Quantification of SMN and Bax expression in (H). (L, M) Quantification of SMN and Bax expression in (I). The experiment was repeated at least three times, and the mean ± SEM was calculated. Statistical comparisons were performed by one-way analysis of variance (ANOVA) (E-G) and Student's t test (B-D, and J-M).* P

    Article Snippet: Primary antibodies used for western blotting included mouse anti-SMN (1:5,000; BD Biosciences, San Diego, CA, USA), mouse anti-β-actin (1:10,000; Sigma), rabbit anti-Bax (1:1,000; Millipore, Temecula, CA, USA), and rabbit anti-caspase 3 (1:1,000; Cell Signaling, Temecula, CA, USA).

    Techniques: Western Blot, Expressing

    Binding partners for Bak and Bcl-w in the mouse mammary gland. (A-C) Equal amounts of tissue extracts from lactating (L9) or apoptotic involuting (I2) mouse mammary gland were precipitated with the indicated reagent and the identity of proteins in the precipitates identified by immunoblotting. In each case samples of lysate were also included on the same gels as positive controls (lysate). (A) Immunoprecipitations were performed with sepharoseconjugated anti-Bak and anti-Bax antibodies or control IgG, and the proteins were separated by SDS-PAGE and transferred to nylon. The blots were probed with antibodies to Bak, Bax and Bcl-w. Note that Bcl-w was not present in Bak immunoprecipitates, but did interact with Bax. No Bcl-w was seen either in whole cell lysates or the Bax immunoprecipitates of the I2 sample. (B) Immunoprecipitations with sepharose-conjugated anti-Bcl-x antibodies were separated by SDS-PAGE, transferred to nylon, and probed with antibodies to Bcl-x or Bak. (C) Tissue extracts were mixed with either GST- or GST-Bcl-w conjugated sepharose beads for 2 hours before centrifugation and separation by SDS-PAGE The gels were transferred to nylon and subjected to immunoblotting using antibodies directed against Bak, Bad and Bax. These data confirm that Bcl-w interacts with Bax but not Bak or Bad in mammary epithelial cells. Note that the I2 lysate contains Bax, which is capable of binding GST-Bcl-w, but the absence of Bcl-w at this developmental stage precludes such an interaction taking place in vivo.

    Journal: Journal of cell science

    Article Title: Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland

    doi:

    Figure Lengend Snippet: Binding partners for Bak and Bcl-w in the mouse mammary gland. (A-C) Equal amounts of tissue extracts from lactating (L9) or apoptotic involuting (I2) mouse mammary gland were precipitated with the indicated reagent and the identity of proteins in the precipitates identified by immunoblotting. In each case samples of lysate were also included on the same gels as positive controls (lysate). (A) Immunoprecipitations were performed with sepharoseconjugated anti-Bak and anti-Bax antibodies or control IgG, and the proteins were separated by SDS-PAGE and transferred to nylon. The blots were probed with antibodies to Bak, Bax and Bcl-w. Note that Bcl-w was not present in Bak immunoprecipitates, but did interact with Bax. No Bcl-w was seen either in whole cell lysates or the Bax immunoprecipitates of the I2 sample. (B) Immunoprecipitations with sepharose-conjugated anti-Bcl-x antibodies were separated by SDS-PAGE, transferred to nylon, and probed with antibodies to Bcl-x or Bak. (C) Tissue extracts were mixed with either GST- or GST-Bcl-w conjugated sepharose beads for 2 hours before centrifugation and separation by SDS-PAGE The gels were transferred to nylon and subjected to immunoblotting using antibodies directed against Bak, Bad and Bax. These data confirm that Bcl-w interacts with Bax but not Bak or Bad in mammary epithelial cells. Note that the I2 lysate contains Bax, which is capable of binding GST-Bcl-w, but the absence of Bcl-w at this developmental stage precludes such an interaction taking place in vivo.

    Article Snippet: Membranes were blocked with 5% skimmed milk (Marvel) in PBS (overnight, 4°C) and incubated (2 hours, RT) with 1.4 μg/ml rabbit anti-Bax, 2 μg/ml mouse anti-Bak (Calbiochem, monoclonal antibody #AM03), 1:250 mouse anti-Bad (Transduction Laboratories, monoclonal antibody # ), 1:500 mouse anti-Bcl-x (Transduction Laboratories, monoclonal antibody # ), 2 μg/ml rabbit anti-Bcl-2 or anti-Bcl-w, or 1:1000 dilution of a monoclonal antibody to β-casein.

    Techniques: Binding Assay, SDS Page, Centrifugation, In Vivo

    High levels of pro-apoptotic Bcl-2 proteins during involution correlate with apoptosis. (A,B) Total RNA was prepared from mammary gland for northern analysis. (A) 10 μg total RNA was blotted onto nylon membranes and hybridised with 32 P-labelled mouse Bax and Bcl-x cDNA. Analysis of β-casein mRNA confirmed that the samples expressed the expected temporal pattern of milk protein genes and an 18S DNA probe was used to assess equal loading of the gels. (B) The blots were analyzed using storage phosphor imaging plates and a Fujix Bas 2000 bioimaging analyzer. The levels of specific mRNA were plotted after normalizing to the level of 18S rRNA. (C) RT-PCR of the cell death genes Bax , Bak and Bad confirmed the RNA profile of Bax as measured by northern blotting and indicated that expression of Bak and Bad were also regulated during development. A 29S ribonuclear protein ( rps29 ) PCR analysis was included to ensure that equal concentrations of RNA were present in the PCR reactions. C, control with no cDNA in the PCR reaction. The faster migrating band in Bak PCR reactions was cloned and sequenced and found to be unrelated to Bak. (D) Multiple bands observed in the involuting day 2 sample of the PCR reaction for Bax were cloned and sequenced. The centrally migrating band corresponded to the major Bax transcript Baxa , while the faster migrating band corresponded to the transcript for Baxγ , which lacks exon 2. The slower migrating band contained a sequence which was unrelated to Bax . (E,F) Whole tissue lysates were prepared from the developmental samples and subjected to polyacrylamide gel electrophoresis. (E) Coomassie staining showed that the protein samples were equally loaded. Western blotting indicated that β-casein was detected in late pregnancy, lactation and early involution, as expected. (F) Similar blots were incubated with antibodies directed against Bax, Bak and Bad. Confirmation of the Bax expression profile was validated using a second independently derived antibody directed against Bax (data not shown). An equal amount of protein from M1 murine myeloid leukaemia cells was included as a positive control for identification of the Bax protein. In each case, and in the subsequent figures, tissue was isolated from 4, 6, or 8 week virgin (v) mice, and at the indicated number of days of pregnancy (P), lactation (L) and involution (I).

    Journal: Journal of cell science

    Article Title: Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland

    doi:

    Figure Lengend Snippet: High levels of pro-apoptotic Bcl-2 proteins during involution correlate with apoptosis. (A,B) Total RNA was prepared from mammary gland for northern analysis. (A) 10 μg total RNA was blotted onto nylon membranes and hybridised with 32 P-labelled mouse Bax and Bcl-x cDNA. Analysis of β-casein mRNA confirmed that the samples expressed the expected temporal pattern of milk protein genes and an 18S DNA probe was used to assess equal loading of the gels. (B) The blots were analyzed using storage phosphor imaging plates and a Fujix Bas 2000 bioimaging analyzer. The levels of specific mRNA were plotted after normalizing to the level of 18S rRNA. (C) RT-PCR of the cell death genes Bax , Bak and Bad confirmed the RNA profile of Bax as measured by northern blotting and indicated that expression of Bak and Bad were also regulated during development. A 29S ribonuclear protein ( rps29 ) PCR analysis was included to ensure that equal concentrations of RNA were present in the PCR reactions. C, control with no cDNA in the PCR reaction. The faster migrating band in Bak PCR reactions was cloned and sequenced and found to be unrelated to Bak. (D) Multiple bands observed in the involuting day 2 sample of the PCR reaction for Bax were cloned and sequenced. The centrally migrating band corresponded to the major Bax transcript Baxa , while the faster migrating band corresponded to the transcript for Baxγ , which lacks exon 2. The slower migrating band contained a sequence which was unrelated to Bax . (E,F) Whole tissue lysates were prepared from the developmental samples and subjected to polyacrylamide gel electrophoresis. (E) Coomassie staining showed that the protein samples were equally loaded. Western blotting indicated that β-casein was detected in late pregnancy, lactation and early involution, as expected. (F) Similar blots were incubated with antibodies directed against Bax, Bak and Bad. Confirmation of the Bax expression profile was validated using a second independently derived antibody directed against Bax (data not shown). An equal amount of protein from M1 murine myeloid leukaemia cells was included as a positive control for identification of the Bax protein. In each case, and in the subsequent figures, tissue was isolated from 4, 6, or 8 week virgin (v) mice, and at the indicated number of days of pregnancy (P), lactation (L) and involution (I).

    Article Snippet: Membranes were blocked with 5% skimmed milk (Marvel) in PBS (overnight, 4°C) and incubated (2 hours, RT) with 1.4 μg/ml rabbit anti-Bax, 2 μg/ml mouse anti-Bak (Calbiochem, monoclonal antibody #AM03), 1:250 mouse anti-Bad (Transduction Laboratories, monoclonal antibody # ), 1:500 mouse anti-Bcl-x (Transduction Laboratories, monoclonal antibody # ), 2 μg/ml rabbit anti-Bcl-2 or anti-Bcl-w, or 1:1000 dilution of a monoclonal antibody to β-casein.

    Techniques: Northern Blot, Imaging, Reverse Transcription Polymerase Chain Reaction, Expressing, Polymerase Chain Reaction, Clone Assay, Sequencing, Polyacrylamide Gel Electrophoresis, Staining, Western Blot, Incubation, Derivative Assay, Positive Control, Isolation, Mouse Assay

    Schematic representation of changes in the expression profiles of Bcl-2 family proteins during mammary development in the pregnancy cycle. Pro-apoptotic proteins are shown in triangles, while death-suppressors are in circles. More triangles/circles indicate a higher level of expression. Note that (1) Bcl-2 expression is absent in lactation and during the time of maximal apoptosis; (2) the death-promoting molecules Bak and Bad are upregulated at the pregnancy/lactation interface and are proposed to prime the gland for apoptosis, while the survival-promoting molecules Bcl-w and Bcl-x maintain mammary gland integrity during lactation; and (3) Bcl-w is downregulated in involution and may therefore allow apoptosis through the action of Bax, Bak and Bad.

    Journal: Journal of cell science

    Article Title: Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland

    doi:

    Figure Lengend Snippet: Schematic representation of changes in the expression profiles of Bcl-2 family proteins during mammary development in the pregnancy cycle. Pro-apoptotic proteins are shown in triangles, while death-suppressors are in circles. More triangles/circles indicate a higher level of expression. Note that (1) Bcl-2 expression is absent in lactation and during the time of maximal apoptosis; (2) the death-promoting molecules Bak and Bad are upregulated at the pregnancy/lactation interface and are proposed to prime the gland for apoptosis, while the survival-promoting molecules Bcl-w and Bcl-x maintain mammary gland integrity during lactation; and (3) Bcl-w is downregulated in involution and may therefore allow apoptosis through the action of Bax, Bak and Bad.

    Article Snippet: Membranes were blocked with 5% skimmed milk (Marvel) in PBS (overnight, 4°C) and incubated (2 hours, RT) with 1.4 μg/ml rabbit anti-Bax, 2 μg/ml mouse anti-Bak (Calbiochem, monoclonal antibody #AM03), 1:250 mouse anti-Bad (Transduction Laboratories, monoclonal antibody # ), 1:500 mouse anti-Bcl-x (Transduction Laboratories, monoclonal antibody # ), 2 μg/ml rabbit anti-Bcl-2 or anti-Bcl-w, or 1:1000 dilution of a monoclonal antibody to β-casein.

    Techniques: Expressing

    ). Equivalent amounts of cell protein were separated by polyacrylamide gel electrophoresis, then analyzed by western immunoblotting. Blots were incubated with antibodies directed against Bax, Bak, Bad, Bcl-x, Bcl-2, Bcl-w and β-casein, and lysates from M1 cells are included as controls.

    Journal: Journal of cell science

    Article Title: Developmental regulation of Bcl-2 family protein expression in the involuting mammary gland

    doi:

    Figure Lengend Snippet: ). Equivalent amounts of cell protein were separated by polyacrylamide gel electrophoresis, then analyzed by western immunoblotting. Blots were incubated with antibodies directed against Bax, Bak, Bad, Bcl-x, Bcl-2, Bcl-w and β-casein, and lysates from M1 cells are included as controls.

    Article Snippet: Membranes were blocked with 5% skimmed milk (Marvel) in PBS (overnight, 4°C) and incubated (2 hours, RT) with 1.4 μg/ml rabbit anti-Bax, 2 μg/ml mouse anti-Bak (Calbiochem, monoclonal antibody #AM03), 1:250 mouse anti-Bad (Transduction Laboratories, monoclonal antibody # ), 1:500 mouse anti-Bcl-x (Transduction Laboratories, monoclonal antibody # ), 2 μg/ml rabbit anti-Bcl-2 or anti-Bcl-w, or 1:1000 dilution of a monoclonal antibody to β-casein.

    Techniques: Polyacrylamide Gel Electrophoresis, Western Blot, Incubation