bax (ProSci Incorporated)

ProSci Incorporated is a verified supplier

ProSci Incorporated manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

ProSci Incorporated bax
$Activation <t>of</t> <t>p53</t> and increased protein expression of proapoptotic Bcl2 molecules after TBI. Western blot analysis of the level of proapoptotic proteins in mouse-injured cortex after TBI. Tissue lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against p53, phosphorylated p53 (Ser 15), PUMA, Noxa, <t>Bax,</t> and β-actin. Levels of p53, phosphorylated p53 (Ser 15), PUMA, Noxa, and Bax were quantified as fold change to control levels after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus sham (N = 4). **p < 0.01 versus sham (N = 4). ***p < 0.001 versus sham (N = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.$
Bax, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+function/HSH2D+Antibody/pmc04107397-333-48-54
Average 91 stars, based on 4 article reviews

bax - by Bioz Stars, 2026-10

91/100 stars

Images

1) Product Images from "Downregulation of miR-23a and miR-27a following Experimental Traumatic Brain Injury Induces Neuronal Cell Death through Activation of Proapoptotic Bcl-2 Proteins"

Article Title: Downregulation of miR-23a and miR-27a following Experimental Traumatic Brain Injury Induces Neuronal Cell Death through Activation of Proapoptotic Bcl-2 Proteins

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.1260-14.2014

$Activation of p53 and increased protein expression of proapoptotic Bcl2 molecules after TBI. Western blot analysis of the level of proapoptotic proteins in mouse-injured cortex after TBI. Tissue lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against p53, phosphorylated p53 (Ser 15), PUMA, Noxa, Bax, and β-actin. Levels of p53, phosphorylated p53 (Ser 15), PUMA, Noxa, and Bax were quantified as fold change to control levels after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus sham (N = 4). **p < 0.01 versus sham (N = 4). ***p < 0.001 versus sham (N = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.$
Figure Legend Snippet: Activation of p53 and increased protein expression of proapoptotic Bcl2 molecules after TBI. Western blot analysis of the level of proapoptotic proteins in mouse-injured cortex after TBI. Tissue lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against p53, phosphorylated p53 (Ser 15), PUMA, Noxa, Bax, and β-actin. Levels of p53, phosphorylated p53 (Ser 15), PUMA, Noxa, and Bax were quantified as fold change to control levels after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus sham (N = 4). **p < 0.01 versus sham (N = 4). ***p < 0.001 versus sham (N = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.

Techniques Used: Activation Assay, Expressing, Western Blot

$mRNA and protein levels of proapoptotic members of Bcl-2 family were increased in etoposide-treated primary cortical neurons. A, qPCR quantification of expression of proapoptotic genes: Noxa, Puma, and Bax in primary cortical neurons at different time points after etoposide treatment. Level of gene expression was normalized to GAPDH expression. Neuronal apoptosis were induced by etoposide as described above. Data are mean ± SD. *p < 0.05 versus control untreated RCNs (N = 4). **p < 0.01 versus control untreated RCNs (N = 4). ***p < 0.001 versus control untreated RCNs (N = 4). B, Western blot analysis of the level of proapoptotic proteins in primary cortical neurons at different time points after etoposide treatment. Cell lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin. Levels of PUMA, Noxa, Bax, and active Bax were quantified as fold change to control levels after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus control untreated RCNs (N = 4). **p < 0.01 versus control untreated RCNs (N = 4). ***p < 0.001 versus control untreated RCNs (N = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.$
Figure Legend Snippet: mRNA and protein levels of proapoptotic members of Bcl-2 family were increased in etoposide-treated primary cortical neurons. A, qPCR quantification of expression of proapoptotic genes: Noxa, Puma, and Bax in primary cortical neurons at different time points after etoposide treatment. Level of gene expression was normalized to GAPDH expression. Neuronal apoptosis were induced by etoposide as described above. Data are mean ± SD. *p < 0.05 versus control untreated RCNs (N = 4). **p < 0.01 versus control untreated RCNs (N = 4). ***p < 0.001 versus control untreated RCNs (N = 4). B, Western blot analysis of the level of proapoptotic proteins in primary cortical neurons at different time points after etoposide treatment. Cell lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin. Levels of PUMA, Noxa, Bax, and active Bax were quantified as fold change to control levels after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus control untreated RCNs (N = 4). **p < 0.01 versus control untreated RCNs (N = 4). ***p < 0.001 versus control untreated RCNs (N = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.

Techniques Used: Expressing, Western Blot

$miR-23a and miR-27a mimics attenuate etoposide-induced expression of proapoptotic Bcl-2 family members. Neurons were transfected with miR-23a-3p and miR-27a-3p mimics and 4 h later treated with etoposide as described above. Whole-cell lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin (A). Levels of PUMA (B), Noxa (C), Bax (D), and active Bax (E) were quantified as fold change to control RCN level after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus mock untreated RCNs. **p < 0.01 versus mock untreated RCNs. ***p < 0.001 versus mock untreated RCNs. +p < 0.05 versus etoposide-treated mock (n = 4). ++p < 0.01 versus etoposide-treated mock (n = 4). +++p < 0.001 versus etoposide-treated mock (n = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.$
Figure Legend Snippet: miR-23a and miR-27a mimics attenuate etoposide-induced expression of proapoptotic Bcl-2 family members. Neurons were transfected with miR-23a-3p and miR-27a-3p mimics and 4 h later treated with etoposide as described above. Whole-cell lysates were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin (A). Levels of PUMA (B), Noxa (C), Bax (D), and active Bax (E) were quantified as fold change to control RCN level after measurement of band intensity by densitometry and normalization to levels of β-actin. Data are mean ± SD. *p < 0.05 versus mock untreated RCNs. **p < 0.01 versus mock untreated RCNs. ***p < 0.001 versus mock untreated RCNs. +p < 0.05 versus etoposide-treated mock (n = 4). ++p < 0.01 versus etoposide-treated mock (n = 4). +++p < 0.001 versus etoposide-treated mock (n = 4). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.

Techniques Used: Expressing, Transfection

miR-23a and miR-27a target PUMA, Noxa, and Bax. SH-SY5Y cells were transfected with either negative control miR (-ve cnt) or miR-23a-3p or miR-27a-3p mimics. Cells were also cotransfected with reporter plasmids with inserted 3′ UTRs of mouse PUMA (A), Noxa (B), and Bax (C). Twenty-four hours after transfection, cells were analyzed for Luciferase activity. Normalized Luciferase activities were shown as the percentage relative to the cells transfected with reporter plasmid and -ve Con miR mimic, which was set as 1. Experiments were performed in triplicate. Data are mean ± SD. **p < 0.01 (n = 3). ***p < 0.001 (n = 3). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.

Figure Legend Snippet: miR-23a and miR-27a target PUMA, Noxa, and Bax. SH-SY5Y cells were transfected with either negative control miR (-ve cnt) or miR-23a-3p or miR-27a-3p mimics. Cells were also cotransfected with reporter plasmids with inserted 3′ UTRs of mouse PUMA (A), Noxa (B), and Bax (C). Twenty-four hours after transfection, cells were analyzed for Luciferase activity. Normalized Luciferase activities were shown as the percentage relative to the cells transfected with reporter plasmid and -ve Con miR mimic, which was set as 1. Experiments were performed in triplicate. Data are mean ± SD. **p < 0.01 (n = 3). ***p < 0.001 (n = 3). Analysis by one-way ANOVA followed by multiple pairwise comparisons using Student-Newman-Keuls post hoc test.

Techniques Used: Transfection, Negative Control, Luciferase, Activity Assay, Plasmid Preparation

$Intracerebroventricular injection of miR-23a and miR-27a mimics attenuate expression of PUMA, Noxa, and Bax in injured cortex after TBI. qPCR quantification of miR-23a-3p, miR-27a-3p (A) and PUMA, Noxa, and Bax (B) expressions in mouse cortex 6 h after TBI and intracerebroventricular injection of miR-23a-3p or miR-27a-3p or negative control miR (-ve Con) mimics. Levels of miRs were normalized to U6 snRNA; levels of PUMA, Noxa, and Bax were normalized to GAPDH. Data are mean ± SD. *p < 0.05 versus sham animals. **p < 0.01 versus sham animals. ***p < 0.001 versus sham animals. +p < 0.05 versus injured -ve Con injected group (N = 4–6). ++p < 0.01 versus injured -ve Con injected group (N = 4–6). C, Whole-tissue lysates from mouse cortex 24 h after TBI and intracerebroventricular injection of miR-23a-3p or miR-27a-3p or -ve cnt mimics were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin. Levels of PUMA, Noxa, Bax, and active Bax in total lysates were quantified as fold change to the levels of sham after measurement of band intensity by densitometry. Data are mean ± SD. *p < 0.05 versus sham animals. **p < 0.01 versus sham animals. ***p < 0.001 versus sham animals. +p < 0.05 versus injured -ve cnt-injected group (N = 4–6). ++p < 0.01 versus injured -ve cnt-injected group (N = 4–6).$
Figure Legend Snippet: Intracerebroventricular injection of miR-23a and miR-27a mimics attenuate expression of PUMA, Noxa, and Bax in injured cortex after TBI. qPCR quantification of miR-23a-3p, miR-27a-3p (A) and PUMA, Noxa, and Bax (B) expressions in mouse cortex 6 h after TBI and intracerebroventricular injection of miR-23a-3p or miR-27a-3p or negative control miR (-ve Con) mimics. Levels of miRs were normalized to U6 snRNA; levels of PUMA, Noxa, and Bax were normalized to GAPDH. Data are mean ± SD. *p < 0.05 versus sham animals. **p < 0.01 versus sham animals. ***p < 0.001 versus sham animals. +p < 0.05 versus injured -ve Con injected group (N = 4–6). ++p < 0.01 versus injured -ve Con injected group (N = 4–6). C, Whole-tissue lysates from mouse cortex 24 h after TBI and intracerebroventricular injection of miR-23a-3p or miR-27a-3p or -ve cnt mimics were fractioned on SDS-polyacrylamide gel and immunoblotted with antibodies against PUMA, Noxa, Bax, active Bax, and β-actin. Levels of PUMA, Noxa, Bax, and active Bax in total lysates were quantified as fold change to the levels of sham after measurement of band intensity by densitometry. Data are mean ± SD. *p < 0.05 versus sham animals. **p < 0.01 versus sham animals. ***p < 0.001 versus sham animals. +p < 0.05 versus injured -ve cnt-injected group (N = 4–6). ++p < 0.01 versus injured -ve cnt-injected group (N = 4–6).

Techniques Used: Injection, Expressing, Negative Control

Incubation:

Article Title: Changes in testicular gene expression following reduced estradiol synthesis: A complex pathway to increased porcine Sertoli cell proliferation.
Article Snippet: .. Rabbit polyclonal antibodies for DLK1 and ADAM17 257 were incubated overnight with rehydrated sections at 4o C at 10 μg/ml in PBS (#7017 and #1131 258 respectively, RRID:AB_2316076 and RRID:AB_203263, Prosci, Poway, CA); the rabbit 259 polyclonal antibody to UNC5CL was similarly incubated with paraffin sections overnight at 4o C 260 at 10 μg/ml (#ALX-210-939, Enzo Life Sciences, Farmingdale, NY, RRID:AB_2052845); the 261 rabbit polyclonal antibody to CCN5 was incubated overnight with rehydrated sections at 4o C 262 (0.5 μg/ml, #500-P212, PeproTech, Rocky Hills, NJ,RRID:AB_1268770). .. Sections were rinsed 263 in PBS and incubated with biotinylated goat anti-rabbit secondary antibody (PK-6101, Vector 264 Laboratories, RRID:AB_2336820).

Western Blot:

Article Title: Transformation by Oncogenic RAS Sensitizes Human Colon Cells to TRAIL-induced Apoptosis by Up-regulating Death Receptor 4 and Death Receptor 5 through a MEK-dependent Pathway
Article Snippet: Immunoblotting—Whole cell lysates were prepared with lysis buffer (50 mM Tris-HCl, pH 7.4, 250 mM sucrose, 1 mM EDTA, 10 mM NaF, 1 mM EGTA, and 1% Triton X-100 supplemented with protease and phosphatase inhibitors, and the lysates were subjected to SDS-PAGE and transferred to nitrocellulose membranes (Bio-Rad). .. Immunoblotting was performed with the following antibodies at 1:1000 (v/v): caspase-8 (Santa Cruz Biotechnology Inc., sc-6134); caspase-3 (Santa Cruz Biotechnology Inc., sc-1225); PARP (Santa Cruz Biotechnology Inc.; sc-8007), p-ERK1/2 (Santa Cruz Biotechnology Inc., sc-7383); ERK-2 (Santa Cruz Biotechnology Inc., sc-1647); p-MEK1/2 (Cell Signaling, no. 9121S); Flip (Alexis, ALX-804-428); TRAIL-R1 (ProSci, no. 1139); TRAIL-R2 (ProSci, no. 2019); FADD (BD Transduction Laboratories, no. 610399); and p-Akt-Ser473 (Cell Signaling, no. 9271S). .. The membranes were scanned with Storm 860 scanner (Amersham Biosciences), and the values were measured using ImageQuant software (Amersham Biosciences).

other:

Article Title: Downregulation of miR-23a and miR-27a following Experimental Traumatic Brain Injury Induces Neuronal Cell Death through Activation of Proapoptotic Bcl-2 Proteins
Article Snippet: Abcam: V5 (ab27674); Histone H2A.X (ab11175); Santa Cruz Biotechnology: AIF (sc-13116); Apaf-1 (sc-65890); cytochrome c (sc-13560); FAS (sc-716); Bim (sc-11425); Cell Signaling Technology: Cleaved Caspase-3 (#9661); Cleaved PARP (#9545); Phospho-Histone H2A.X (Ser139) (#9718); Phospho-p53 (Ser15) (#9284); p53 (1C12) (#2524); Bax (#2772); XIAP (#2042); Enzo Life Sciences: GAPDH (ADI-CSA-335); Bax (active monomer) (ALX-804-224-C100); α-fodrin (BML-FG6090); ProSci: PUMA (#3041); Noxa (#2437); EMD Millipore: Bak (06-536); Sigma: β-actin (A1978).

Review