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Promega mouse monoclonal antibody
Mouse Monoclonal Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 97/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse monoclonal antibody/product/Promega
Average 97 stars, based on 35 article reviews
Price from $9.99 to $1999.99

mouse monoclonal antibody - by Bioz Stars, 2022-08

97/100 stars

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ß tubulin iii (Promega)

Promega ß tubulin iii

Differentiation assays. (a) Left: Adipocyte with lipid vacuole resulted from adipogenic differentiation of CD146 positive cell stained with oil red. Right: Expression of PAPR‐γ2 and aP‐2 is shown following adipogenic differentiation using PCR. (b) Left: Mineralization and appropriate morphological changes are shown following osteogenic differentiation stained with alizarin red. Right: With osteogenic differentiation, expression of OPN and Col1α1 is revealed by PCR. (c) Left: With neurogenic differentiation typical dendritic cells which express appeared Right: <t>ß‐tubulin</t> III revealed by immune‐fluorescent staining. (d) Left: With hepatocytic differentiation, polygonal/flattened shape cells appeared at day 21 (differentiation step 2) Right: Hepatogenic differentiation was confirmed by qRT‐PCR as hepatogenic related genes were upregulated postdifferentiation, specially ALB and HNF with approximately 10‐ and 2.5‐fold higher expression after differentiation. The bars represent gene expressions before and after differentiation

ß Tubulin Iii, supplied by Promega, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ß tubulin iii/product/Promega
Average 97 stars, based on 1 article reviews
Price from $9.99 to $1999.99

ß tubulin iii - by Bioz Stars, 2022-08

97/100 stars

Buy from Supplier

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Journal: Clinical and Experimental Dental Research

Article Title: Differential expression of drug resistance genes in CD146 positive dental pulp derived stem cells and CD146 negative fibroblasts, et al. Differential expression of drug resistance genes in CD146 positive dental pulp derived stem cells and CD146 negative fibroblasts

doi: 10.1002/cre2.297

Figure Lengend Snippet: Differentiation assays. (a) Left: Adipocyte with lipid vacuole resulted from adipogenic differentiation of CD146 positive cell stained with oil red. Right: Expression of PAPR‐γ2 and aP‐2 is shown following adipogenic differentiation using PCR. (b) Left: Mineralization and appropriate morphological changes are shown following osteogenic differentiation stained with alizarin red. Right: With osteogenic differentiation, expression of OPN and Col1α1 is revealed by PCR. (c) Left: With neurogenic differentiation typical dendritic cells which express appeared Right: ß‐tubulin III revealed by immune‐fluorescent staining. (d) Left: With hepatocytic differentiation, polygonal/flattened shape cells appeared at day 21 (differentiation step 2) Right: Hepatogenic differentiation was confirmed by qRT‐PCR as hepatogenic related genes were upregulated postdifferentiation, specially ALB and HNF with approximately 10‐ and 2.5‐fold higher expression after differentiation. The bars represent gene expressions before and after differentiation

Article Snippet: To confirm neural differentiation, immunostaining was performed for ß‐tubulin III (Promega cat number: G7121) as a specific antibody against neurons.

Techniques: Staining, Expressing, Polymerase Chain Reaction, Quantitative RT-PCR

FAST enhances the expression of cotransfected β-galactosidase. The left panel shows COS-7 cells cotransfected with a β-galactosidase reporter together with pMT2 alone, pMT2-HA-FAST, pMT2-HA-TIA-1, or pMT2-HA-TIA-1-PRD. After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase (β-gal). The right panel shows COS-7 cells cotransfected with a β-galactosidase reporter together with pMT2-HA-FAST and increasing amounts of pMT2-HA-TIA-1 (5:1, 2:1, 1:1). After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase and the expression of recombinant TIA-1 and FAST.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: FAST enhances the expression of cotransfected β-galactosidase. The left panel shows COS-7 cells cotransfected with a β-galactosidase reporter together with pMT2 alone, pMT2-HA-FAST, pMT2-HA-TIA-1, or pMT2-HA-TIA-1-PRD. After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase (β-gal). The right panel shows COS-7 cells cotransfected with a β-galactosidase reporter together with pMT2-HA-FAST and increasing amounts of pMT2-HA-TIA-1 (5:1, 2:1, 1:1). After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase and the expression of recombinant TIA-1 and FAST.

Article Snippet: Antibodies obtained from commercial sources include antihemagglutinin (anti-HA) (murine monoclonal antibody clone 16B12, immunoglobulin G1; Berkeley Antibody Co.), anti-FLAG (murine monoclonal antibody clone; Sigma Chemical Co., St. Louis, Mo.), anti-BCL-XL (rabbit polyclonal and mouse monoclonal; Santa Cruz Biotechnology, Inc.), anti-Myc (rabbit polyclonal; Santa Cruz Biotechnology, Inc.), anti-active caspase 3 (rabbit polyclonal; Promega), rabbit polyclonal anti-cIAP-1 (R and D), mouse monoclonal anti-XIAP (Stressgen), mouse monoclonal anti-GAPDH (Research Diagnostics), and anti-β-galactosidase (mouse monoclonal; Promega).

Techniques: Expressing, Western Blot, Recombinant

FAST inhibits Fas- and UV-induced apoptosis. (A) HeLa cells were mock transfected or transfected with vectors encoding HA-FAST or β-galactosidase, cultured in the absence (untreated) or presence of anti-Fas antibody (FAS) before being processed for immunofluorescence microscopy using anti-HA, anti-β-galactosidase, anti-active caspase 3, and Hoechst dye. Arrows point out cells undergoing Fas-induced caspase-dependent apoptosis. Arrowheads point out FAST transfectants in which caspase 3 is not activated. Size bar, 20 μm. (B) HeLa cells were mock transfected or transfected with either FAST or β-galactosidase (β-gal), cultured in the presence of anti-Fas antibody, and then processed for TUNEL analysis (red) and immunofluorescence (anti-HA, green; anti-active caspase 3, blue) or Hoechst staining. Arrows point out untransfected cells or β-galactosidase-transfected cells. Arrowheads point out FAST transfectants. (C) The mean percentages (±standard errors; n = 3) of transfected cells (vector control, HA-FAST, HA-FASTN, or HA-FASTC; revealed using anti-HA or anti-β-galactosidase) cultured under the indicated conditions that exhibit active caspase 3 are presented as a bar graph. Calculated P values for selected comparisons are shown.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: FAST inhibits Fas- and UV-induced apoptosis. (A) HeLa cells were mock transfected or transfected with vectors encoding HA-FAST or β-galactosidase, cultured in the absence (untreated) or presence of anti-Fas antibody (FAS) before being processed for immunofluorescence microscopy using anti-HA, anti-β-galactosidase, anti-active caspase 3, and Hoechst dye. Arrows point out cells undergoing Fas-induced caspase-dependent apoptosis. Arrowheads point out FAST transfectants in which caspase 3 is not activated. Size bar, 20 μm. (B) HeLa cells were mock transfected or transfected with either FAST or β-galactosidase (β-gal), cultured in the presence of anti-Fas antibody, and then processed for TUNEL analysis (red) and immunofluorescence (anti-HA, green; anti-active caspase 3, blue) or Hoechst staining. Arrows point out untransfected cells or β-galactosidase-transfected cells. Arrowheads point out FAST transfectants. (C) The mean percentages (±standard errors; n = 3) of transfected cells (vector control, HA-FAST, HA-FASTN, or HA-FASTC; revealed using anti-HA or anti-β-galactosidase) cultured under the indicated conditions that exhibit active caspase 3 are presented as a bar graph. Calculated P values for selected comparisons are shown.

Techniques: Transfection, Cell Culture, Immunofluorescence, Microscopy, TUNEL Assay, Staining, Plasmid Preparation

Effects of siFAST-1 on β-galactosidase expression. COS-7 cells were cotransfected with a β-galactosidase (β-gal) reporter together with pMT2-HA-FAST, pMT2-HA-FASTN, or pMT2-HA-FASTC and either pSupressor2-siNC (lanes 1 to 3) or pSupressor-2-siFAST-1 (lanes 4 to 6). After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase (A) or individual HA-FAST constructs (B). Molecular size markers are shown at the left. Bands corresponding to β-galactosidase, HA-FAST, and HA-FASTC are indicated by arrows.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: Effects of siFAST-1 on β-galactosidase expression. COS-7 cells were cotransfected with a β-galactosidase (β-gal) reporter together with pMT2-HA-FAST, pMT2-HA-FASTN, or pMT2-HA-FASTC and either pSupressor2-siNC (lanes 1 to 3) or pSupressor-2-siFAST-1 (lanes 4 to 6). After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase (A) or individual HA-FAST constructs (B). Molecular size markers are shown at the left. Bands corresponding to β-galactosidase, HA-FAST, and HA-FASTC are indicated by arrows.

Techniques: Expressing, Western Blot, Construct

Fas ligation modulates the expression of β-galactosidase. (A) HeLa cells were cotransfected with a β-galactosidase reporter together with pMT2 vector, pMT2-HA-FAST, or pMT2-HA-FASTC, and then they were cultured in the absence or presence of anti-Fas antibody before being processed for Western blotting analysis to quantify the expression of β-galactosidase (β-gal) (upper panel), HA-FAST, and HA-FASTC (lower panel). (B) HeLa cells were transfected with negative control siRNA or siFAST-1 and cultured for 28 or 36 h in the presence of z-VAD (100 nM; Enzyme Systems Products), and then they were treated with anti-Fas antibody for 6 h or overnight, as indicated, before being processed for immunoblotting analysis to quantify the expression of β-galactosidase and endogenous GAPDH.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: Fas ligation modulates the expression of β-galactosidase. (A) HeLa cells were cotransfected with a β-galactosidase reporter together with pMT2 vector, pMT2-HA-FAST, or pMT2-HA-FASTC, and then they were cultured in the absence or presence of anti-Fas antibody before being processed for Western blotting analysis to quantify the expression of β-galactosidase (β-gal) (upper panel), HA-FAST, and HA-FASTC (lower panel). (B) HeLa cells were transfected with negative control siRNA or siFAST-1 and cultured for 28 or 36 h in the presence of z-VAD (100 nM; Enzyme Systems Products), and then they were treated with anti-Fas antibody for 6 h or overnight, as indicated, before being processed for immunoblotting analysis to quantify the expression of β-galactosidase and endogenous GAPDH.

Techniques: Ligation, Expressing, Plasmid Preparation, Cell Culture, Western Blot, Transfection, Negative Control

Knocking down FAST results in apoptosis. (A) COS-7 cells were transfected with pMT2-HA-FAST together with a vector-based negative control RNAi (pSuppressor2-SiNC), FAST RNAi-1 (pSuppressor2-SiFAST-1), or FAST RNAi-2 (pSupressor2-SiFAST-2). After 48 h, cells were processed for Western blotting analysis to quantify the expression of recombinant HA-FAST. (B) HeLa cells were transfected with either negative control RNAi (SiNC) or FAST RNAi (SiFAST-1). After 48 h, cells were processed for Western blotting analysis to quantify the expression of endogenous FAST. (C) HeLa cells were transfected with pcDNA3-β-galactosidase together with either negative control RNAi (SiNC) or FAST RNAi (siFAST-1 or siFAST-2) before being processed for immunofluorescence microscopy using anti-β-galactosidase, anti-active caspase 3, or Hoechst dye. Arrows point out healthy transfected cells. Arrowheads point out transfected cells that are undergoing apoptosis. Size bar, 20 μm. (D) The mean percentages (±standard errors; n = 3) of transfected cells (revealed using anti-β-galactosidase) that exhibit active caspase-3 are presented as a bar graph. Calculated P values for selected comparisons are shown. β-gal, β-galactosidase.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: Knocking down FAST results in apoptosis. (A) COS-7 cells were transfected with pMT2-HA-FAST together with a vector-based negative control RNAi (pSuppressor2-SiNC), FAST RNAi-1 (pSuppressor2-SiFAST-1), or FAST RNAi-2 (pSupressor2-SiFAST-2). After 48 h, cells were processed for Western blotting analysis to quantify the expression of recombinant HA-FAST. (B) HeLa cells were transfected with either negative control RNAi (SiNC) or FAST RNAi (SiFAST-1). After 48 h, cells were processed for Western blotting analysis to quantify the expression of endogenous FAST. (C) HeLa cells were transfected with pcDNA3-β-galactosidase together with either negative control RNAi (SiNC) or FAST RNAi (siFAST-1 or siFAST-2) before being processed for immunofluorescence microscopy using anti-β-galactosidase, anti-active caspase 3, or Hoechst dye. Arrows point out healthy transfected cells. Arrowheads point out transfected cells that are undergoing apoptosis. Size bar, 20 μm. (D) The mean percentages (±standard errors; n = 3) of transfected cells (revealed using anti-β-galactosidase) that exhibit active caspase-3 are presented as a bar graph. Calculated P values for selected comparisons are shown. β-gal, β-galactosidase.

Techniques: Transfection, Plasmid Preparation, Negative Control, Western Blot, Expressing, Recombinant, Immunofluorescence, Microscopy

FASTC increases reporter gene expression and is regulated by BCL-X L . (A) COS-7 cells were cotransfected with a β-galactosidase reporter together with pcDNA3 vector and pMT2 alone, pMT2-HA-FAST, pMT2-HA-FASTN, pMT2-HA-FASTC, or pMT2-HA-FASTCΔBH3. After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase. (B) COS-7 cells were cotransfected with a β-galactosidase reporter together with pcDNA3-BCL-X L and pMT2 alone, pMT2-HA-FAST, pMT2-HA-FASTN, or pMT2-HA-FASTC.

Journal: Molecular and Cellular Biology

Article Title: FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

doi: 10.1128/MCB.24.24.10718-10732.2004

Figure Lengend Snippet: FASTC increases reporter gene expression and is regulated by BCL-X L . (A) COS-7 cells were cotransfected with a β-galactosidase reporter together with pcDNA3 vector and pMT2 alone, pMT2-HA-FAST, pMT2-HA-FASTN, pMT2-HA-FASTC, or pMT2-HA-FASTCΔBH3. After 48 h, cells were processed for Western blotting analysis to quantify the expression of β-galactosidase. (B) COS-7 cells were cotransfected with a β-galactosidase reporter together with pcDNA3-BCL-X L and pMT2 alone, pMT2-HA-FAST, pMT2-HA-FASTN, or pMT2-HA-FASTC.

Techniques: Expressing, Plasmid Preparation, Western Blot

Differentiation of primary neurospheres. A-C , Representative differentiated neurospheres immunolabeled for GFAP (green) and βIII tubulin (red) and counterstained with DAPI (blue). Primary pLV neurosphere ( A ), primary hippocampal neurosphere grown in the presence of EGF and FGF-2 ( B ), and a primary hippocampal neurosphere cultured in the presence of EGF, FGF-2, and BDNF (100 ng/ml) ( C ) are shown. A , B , Insets, Immunolabeling for the oligodendrocyte marker O4 (green) in representative differentiated pLV ( A ) and hippocampal ( B ) neurospheres. D , Percentage of differentiated neurospheres containing cells immunopositive for either GFAP alone (astrocytes) or GFAP plus βIII tubulin (neurons) after growth in the presence of EGF and FGF-2 or with BDNF (100 ng/ml) added to hippocampal cultures at different time points during neurosphere proliferation ( n = 3; mean ± SEM). E , Percentage of differentiated neurospheres containing astrocytes alone or astrocytes plus neurons when primary hippocampal cells were cultured in increasing concentrations of BDNF ( n = 3; mean ± SEM). Hippo., Hippocampus.

Journal: The Journal of Neuroscience

Article Title: The Adult Mouse Hippocampal Progenitor Is Neurogenic But Not a Stem Cell

doi: 10.1523/JNEUROSCI.3249-05.2005

Figure Lengend Snippet: Differentiation of primary neurospheres. A-C , Representative differentiated neurospheres immunolabeled for GFAP (green) and βIII tubulin (red) and counterstained with DAPI (blue). Primary pLV neurosphere ( A ), primary hippocampal neurosphere grown in the presence of EGF and FGF-2 ( B ), and a primary hippocampal neurosphere cultured in the presence of EGF, FGF-2, and BDNF (100 ng/ml) ( C ) are shown. A , B , Insets, Immunolabeling for the oligodendrocyte marker O4 (green) in representative differentiated pLV ( A ) and hippocampal ( B ) neurospheres. D , Percentage of differentiated neurospheres containing cells immunopositive for either GFAP alone (astrocytes) or GFAP plus βIII tubulin (neurons) after growth in the presence of EGF and FGF-2 or with BDNF (100 ng/ml) added to hippocampal cultures at different time points during neurosphere proliferation ( n = 3; mean ± SEM). E , Percentage of differentiated neurospheres containing astrocytes alone or astrocytes plus neurons when primary hippocampal cells were cultured in increasing concentrations of BDNF ( n = 3; mean ± SEM). Hippo., Hippocampus.

Article Snippet: The blocking solution was replaced with fresh blocking solution containing either mouse monoclonal βIII tubulin antibody (1:2000; Promega, Madison, WI) plus rabbit polyclonal GFAP antibody (1:500; DakoCytomation, Carpinteria, CA) or mouse monoclonal O4 antibody (1:100; Chemicon, Boronia, Australia) and incubated for 60 min at room temperature.

Techniques: Immunolabeling, Cell Culture, Marker

Effect of disease mutations on protein stability and protein-protein interactions. (a) Western blotting with anti-GFP antibody confirming the protein expression levels of wild-type Rrm2b, Actn2, Hprt1, Pnp, Tpk1, Gnmt, Gale, Fbp1, Klhl3, Tp53, Pnp, Smad4, and corresponding mutant alleles. β-tubulin and γ-tubulin were used as loading controls. Red denotes “interface residue” mutations, orange denotes “interface domain” mutations and blue denotes “away from the interface” mutations. (b) Likelihood of disruption of interactions by “interface residue”, “interface domain” and “away from the interface” mutations – overall and for stable mutants only; likelihood of a disease mutation disrupting a given interaction in the absence of structural information. Error bars indicate +SE. ( N = 204 mutations).

Journal: PLoS Genetics

Article Title: A Massively Parallel Pipeline to Clone DNA Variants and Examine Molecular Phenotypes of Human Disease Mutations

doi: 10.1371/journal.pgen.1004819

Figure Lengend Snippet: Effect of disease mutations on protein stability and protein-protein interactions. (a) Western blotting with anti-GFP antibody confirming the protein expression levels of wild-type Rrm2b, Actn2, Hprt1, Pnp, Tpk1, Gnmt, Gale, Fbp1, Klhl3, Tp53, Pnp, Smad4, and corresponding mutant alleles. β-tubulin and γ-tubulin were used as loading controls. Red denotes “interface residue” mutations, orange denotes “interface domain” mutations and blue denotes “away from the interface” mutations. (b) Likelihood of disruption of interactions by “interface residue”, “interface domain” and “away from the interface” mutations – overall and for stable mutants only; likelihood of a disease mutation disrupting a given interaction in the absence of structural information. Error bars indicate +SE. ( N = 204 mutations).

Article Snippet: Anti-HA (Sigma H9658), anti-V5 (Invitrogen 46-0705), anti-β-tubulin (Promega G7121), and anti-GFP (Santa Cruz sc-9996) antibodies were used at 1∶3,000 dilutions for immunoblotting analysis.

Techniques: Western Blot, Expressing, Mutagenesis