mouse anti tubulin beta3 antibodies Search Results


mouse anti beta tubulin iii  (Bio-Rad)
94
Bio-Rad mouse anti beta tubulin iii
Mouse Anti Beta Tubulin Iii, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti α tubulin  (Boster Bio)
96
Boster Bio mouse anti α tubulin
Mouse Anti α Tubulin, supplied by Boster Bio, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti β  (StressMarq)
93
StressMarq anti β
Anti β, supplied by StressMarq, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
anti β - by Bioz Stars, 2026-09
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β subunit  (StressMarq)
90
StressMarq β subunit
β Subunit, supplied by StressMarq, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β subunit - by Bioz Stars, 2026-09
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rab bit anti mouse laminin 5 chain antibodies  (Valiant Co Ltd)
97
Valiant Co Ltd rab bit anti mouse laminin 5 chain antibodies
Rab Bit Anti Mouse Laminin 5 Chain Antibodies, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti β3 subunit  (NeuroMab)
94
NeuroMab mouse anti β3 subunit
Mouse Anti β3 Subunit, supplied by NeuroMab, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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polyclonal anti laminin 332 β chain antibodies  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology polyclonal anti laminin 332 β chain antibodies
Polyclonal Anti Laminin 332 β Chain Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+tubulin+beta3+antibodies/Laminin/pmc06048497-505-6-37
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recombinant hu man tgf b3  (R&D Systems)
93
R&D Systems recombinant hu man tgf b3
Recombinant Hu Man Tgf B3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+tubulin+beta3+antibodies/TGF-beta+3+Antibody/10__1093_slash_clinchem_slash_43__10__1965-59-6-31
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anti mouse tgfβ 3 blocking antibody  (R&D Systems)
91
R&D Systems anti mouse tgfβ 3 blocking antibody
Anti Mouse Tgfβ 3 Blocking Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β3 integrin  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc β3 integrin
Figure 4. Mmp9/Mmp14 regulates galectin-3 lattice remodeling in osteoclasts. (A and B) Galectin-3 expression and cleavage as assessed with anti–galectin-3 monoclonal antibody (ab2785; Abcam; epitopes mapped against N-terminal region) by Western blot (A) and quantification (B) in BMDMs and osteoclasts (OC) generated from wild-type or DKO mice. Data are presented as mean ± SEM (n = <t>3</t> biological replicates). (C and D) Galectin-3 (green) im- munofluorescence of non-permeabilized wild-type or DKO osteoclasts stained with an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38, epitopes mapped against N-terminal region; C), and surface galectin-3 level quantified (D). Scale bar, 20 μm. Data are presented as mean ± SEM (n = 3 biological replicates with two technical replicates each). (E) Following cell surface biotinylation and capture with streptavidin magnetic beads, Mmp9, Mmp14, galectin-3, and β3 <t>integrin</t> expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. (F) Measurements of surface galectin-3 in wild-type and DKO osteoclasts with eFluor 660–conjugated anti–galectin-3 monoclonal antibody (#50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal domain) by flow cytometry. Results are representative of three independent experiments. (G) Measurements of surface galectin-1 in wild-type and DKO osteoclasts by flow cytometry. Results are representative of three independent experiments. (H) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP9, an MMP9E/A mutant, or an empty control, and differentiated into osteoclasts. Cell lysates were collected for MMP9 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. (I) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP14, MMP14E/A, or an empty control and differentiated into osteoclasts. Cell lysates were collected for MMP14 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using two-way ANOVA with Bonferroni cor- rection (B) and unpaired two-sided Student’s t test (D). Source data are available for this figure: SourceData F4.
β3 Integrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+tubulin+beta3+antibodies/Integrin+beta3+Antibody/pm36880731-343-70-76
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anti tubulin antibody  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti tubulin antibody
Figure 4. Mmp9/Mmp14 regulates galectin-3 lattice remodeling in osteoclasts. (A and B) Galectin-3 expression and cleavage as assessed with anti–galectin-3 monoclonal antibody (ab2785; Abcam; epitopes mapped against N-terminal region) by Western blot (A) and quantification (B) in BMDMs and osteoclasts (OC) generated from wild-type or DKO mice. Data are presented as mean ± SEM (n = <t>3</t> biological replicates). (C and D) Galectin-3 (green) im- munofluorescence of non-permeabilized wild-type or DKO osteoclasts stained with an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38, epitopes mapped against N-terminal region; C), and surface galectin-3 level quantified (D). Scale bar, 20 μm. Data are presented as mean ± SEM (n = 3 biological replicates with two technical replicates each). (E) Following cell surface biotinylation and capture with streptavidin magnetic beads, Mmp9, Mmp14, galectin-3, and β3 <t>integrin</t> expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. (F) Measurements of surface galectin-3 in wild-type and DKO osteoclasts with eFluor 660–conjugated anti–galectin-3 monoclonal antibody (#50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal domain) by flow cytometry. Results are representative of three independent experiments. (G) Measurements of surface galectin-1 in wild-type and DKO osteoclasts by flow cytometry. Results are representative of three independent experiments. (H) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP9, an MMP9E/A mutant, or an empty control, and differentiated into osteoclasts. Cell lysates were collected for MMP9 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. (I) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP14, MMP14E/A, or an empty control and differentiated into osteoclasts. Cell lysates were collected for MMP14 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using two-way ANOVA with Bonferroni cor- rection (B) and unpaired two-sided Student’s t test (D). Source data are available for this figure: SourceData F4.
Anti Tubulin Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+tubulin+beta3+antibodies/beta3-Tubulin+XP+Rabbit+mAb/pm38056894-50-75-79
Average 96 stars, based on 1 article reviews
anti tubulin antibody - by Bioz Stars, 2026-09
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mouse anti βiii tubulin  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc mouse anti βiii tubulin
Figure 4. Mmp9/Mmp14 regulates galectin-3 lattice remodeling in osteoclasts. (A and B) Galectin-3 expression and cleavage as assessed with anti–galectin-3 monoclonal antibody (ab2785; Abcam; epitopes mapped against N-terminal region) by Western blot (A) and quantification (B) in BMDMs and osteoclasts (OC) generated from wild-type or DKO mice. Data are presented as mean ± SEM (n = <t>3</t> biological replicates). (C and D) Galectin-3 (green) im- munofluorescence of non-permeabilized wild-type or DKO osteoclasts stained with an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38, epitopes mapped against N-terminal region; C), and surface galectin-3 level quantified (D). Scale bar, 20 μm. Data are presented as mean ± SEM (n = 3 biological replicates with two technical replicates each). (E) Following cell surface biotinylation and capture with streptavidin magnetic beads, Mmp9, Mmp14, galectin-3, and β3 <t>integrin</t> expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. (F) Measurements of surface galectin-3 in wild-type and DKO osteoclasts with eFluor 660–conjugated anti–galectin-3 monoclonal antibody (#50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal domain) by flow cytometry. Results are representative of three independent experiments. (G) Measurements of surface galectin-1 in wild-type and DKO osteoclasts by flow cytometry. Results are representative of three independent experiments. (H) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP9, an MMP9E/A mutant, or an empty control, and differentiated into osteoclasts. Cell lysates were collected for MMP9 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. (I) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP14, MMP14E/A, or an empty control and differentiated into osteoclasts. Cell lysates were collected for MMP14 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using two-way ANOVA with Bonferroni cor- rection (B) and unpaired two-sided Student’s t test (D). Source data are available for this figure: SourceData F4.
Mouse Anti βiii Tubulin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+tubulin+beta3+antibodies/beta3-Tubulin+(TU-20)+Mouse+mAb/pmc11011893-70-42-45
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Image Search Results


Figure 4. Mmp9/Mmp14 regulates galectin-3 lattice remodeling in osteoclasts. (A and B) Galectin-3 expression and cleavage as assessed with anti–galectin-3 monoclonal antibody (ab2785; Abcam; epitopes mapped against N-terminal region) by Western blot (A) and quantification (B) in BMDMs and osteoclasts (OC) generated from wild-type or DKO mice. Data are presented as mean ± SEM (n = 3 biological replicates). (C and D) Galectin-3 (green) im- munofluorescence of non-permeabilized wild-type or DKO osteoclasts stained with an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38, epitopes mapped against N-terminal region; C), and surface galectin-3 level quantified (D). Scale bar, 20 μm. Data are presented as mean ± SEM (n = 3 biological replicates with two technical replicates each). (E) Following cell surface biotinylation and capture with streptavidin magnetic beads, Mmp9, Mmp14, galectin-3, and β3 integrin expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. (F) Measurements of surface galectin-3 in wild-type and DKO osteoclasts with eFluor 660–conjugated anti–galectin-3 monoclonal antibody (#50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal domain) by flow cytometry. Results are representative of three independent experiments. (G) Measurements of surface galectin-1 in wild-type and DKO osteoclasts by flow cytometry. Results are representative of three independent experiments. (H) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP9, an MMP9E/A mutant, or an empty control, and differentiated into osteoclasts. Cell lysates were collected for MMP9 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. (I) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP14, MMP14E/A, or an empty control and differentiated into osteoclasts. Cell lysates were collected for MMP14 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using two-way ANOVA with Bonferroni cor- rection (B) and unpaired two-sided Student’s t test (D). Source data are available for this figure: SourceData F4.

Journal: The Journal of cell biology

Article Title: Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption.

doi: 10.1083/jcb.202206121

Figure Lengend Snippet: Figure 4. Mmp9/Mmp14 regulates galectin-3 lattice remodeling in osteoclasts. (A and B) Galectin-3 expression and cleavage as assessed with anti–galectin-3 monoclonal antibody (ab2785; Abcam; epitopes mapped against N-terminal region) by Western blot (A) and quantification (B) in BMDMs and osteoclasts (OC) generated from wild-type or DKO mice. Data are presented as mean ± SEM (n = 3 biological replicates). (C and D) Galectin-3 (green) im- munofluorescence of non-permeabilized wild-type or DKO osteoclasts stained with an anti–galectin-3 monoclonal antibody (#125401; Biolegend; clone M3/38, epitopes mapped against N-terminal region; C), and surface galectin-3 level quantified (D). Scale bar, 20 μm. Data are presented as mean ± SEM (n = 3 biological replicates with two technical replicates each). (E) Following cell surface biotinylation and capture with streptavidin magnetic beads, Mmp9, Mmp14, galectin-3, and β3 integrin expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. (F) Measurements of surface galectin-3 in wild-type and DKO osteoclasts with eFluor 660–conjugated anti–galectin-3 monoclonal antibody (#50-5301-82; Thermo Fisher Scientific; clone M3/38, epitopes mapped within the N-terminal domain) by flow cytometry. Results are representative of three independent experiments. (G) Measurements of surface galectin-1 in wild-type and DKO osteoclasts by flow cytometry. Results are representative of three independent experiments. (H) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP9, an MMP9E/A mutant, or an empty control, and differentiated into osteoclasts. Cell lysates were collected for MMP9 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. (I) DKO BMDMs were transduced with lentiviral vectors expressing full-length MMP14, MMP14E/A, or an empty control and differentiated into osteoclasts. Cell lysates were collected for MMP14 and galectin-3 expression and cleavage as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using two-way ANOVA with Bonferroni cor- rection (B) and unpaired two-sided Student’s t test (D). Source data are available for this figure: SourceData F4.

Article Snippet: Antigen detection was performed using antibodies directed against c-Src (rabbit antimouse/human antibody; #2109; Cell Signaling), Ctsk (mouse anti-mouse/human antibody; sc-48353; Santa Cruz), Rho (mouse anti-mouse/human antibody; #05-778; Millipore), galectin-3 (mouse anti-mouse/human antibody; ab2785; Abcam; epitopes mapped within the N-terminal region), Lrp1 (mouse anti-mouse antibody; MABN1796; Millipore), Mmp9 (rabbit anti-mouse antibody; ab38898; Abcam), Mmp14 (rabbit anti-mouse antibody; ab53712; Abcam), OXPHOS (rabbit anti-mouse antibody; ab110413; Abcam), vinculin (mouse anti-mouse antibody; V9131; Sigma-Aldrich), β3 integrin (rabbit anti-mouse antibody; #4702; Cell Signaling), or β-actin (rabbit anti-mouse antibody; #4970; Cell Signaling).

Techniques: Expressing, Western Blot, Generated, Staining, Magnetic Beads, Membrane, Flow Cytometry, Transduction, Mutagenesis, Control

Figure 7. Mmp9/Mmp14 co-dependent regulation of osteoclast function through the galectin-3–centric control of Lrp1 activation. (A–C) Pre- osteoclasts were incubated with either human GALECTIN-3 or GALECTIN-3-biotin (hGAL3-biotin; 1.5 µM) for 30 min at 4°C. Biotinylated GALECTIN-3 was precipitated with streptavidin magnetic beads, separated by SDS-PAGE (A), and analyzed by mass spectrometry (B). Hits were classified according to the peptides spectral matches and the number of peptides per protein. Red columns: the top hit of GALECTIN-3 binding partner. The numbering on the x axis relates to Table S3. Pie chart depicts GALECTIN-3 interactors based on the GO annotation “cellular component” in FunRich (C). (D) Lrp1 and galectin-3 ex- pression from the above streptavidin magnetic beads–precipitated lysates as assessed by Western blot. Results are representative of three independent experiments. (E) Protein lysates from wild-type osteoclasts were immunoprecipitated with the galectin-3 antibody, and Lrp1 and galectin-3 levels assessed by Western blot. Results are representative of three independent experiments. (F and G) Cell-free binding assay demonstrating direct binding between 0.1 and 3.2 μg GALECTIN-3 and 0.5 μg LRP1 for 4 h at 30°C (F), and the competitive inhibition of binding between GALECTIN-3 and LRP1 (1.6 versus 0.5 μg) by 50 mM sucrose, 50 mM lactose, or 10 mg/ml GCS-100 (G). Data are presented as mean ± SEM (n = 3 biological replicates). (H) Following cell surface biotinylation and capture with streptavidin magnetic beads, Lrp1 and β3 integrin expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using one-way ANOVA with Bonferroni correction. Source data are available for this figure: SourceData F7.

Journal: The Journal of cell biology

Article Title: Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption.

doi: 10.1083/jcb.202206121

Figure Lengend Snippet: Figure 7. Mmp9/Mmp14 co-dependent regulation of osteoclast function through the galectin-3–centric control of Lrp1 activation. (A–C) Pre- osteoclasts were incubated with either human GALECTIN-3 or GALECTIN-3-biotin (hGAL3-biotin; 1.5 µM) for 30 min at 4°C. Biotinylated GALECTIN-3 was precipitated with streptavidin magnetic beads, separated by SDS-PAGE (A), and analyzed by mass spectrometry (B). Hits were classified according to the peptides spectral matches and the number of peptides per protein. Red columns: the top hit of GALECTIN-3 binding partner. The numbering on the x axis relates to Table S3. Pie chart depicts GALECTIN-3 interactors based on the GO annotation “cellular component” in FunRich (C). (D) Lrp1 and galectin-3 ex- pression from the above streptavidin magnetic beads–precipitated lysates as assessed by Western blot. Results are representative of three independent experiments. (E) Protein lysates from wild-type osteoclasts were immunoprecipitated with the galectin-3 antibody, and Lrp1 and galectin-3 levels assessed by Western blot. Results are representative of three independent experiments. (F and G) Cell-free binding assay demonstrating direct binding between 0.1 and 3.2 μg GALECTIN-3 and 0.5 μg LRP1 for 4 h at 30°C (F), and the competitive inhibition of binding between GALECTIN-3 and LRP1 (1.6 versus 0.5 μg) by 50 mM sucrose, 50 mM lactose, or 10 mg/ml GCS-100 (G). Data are presented as mean ± SEM (n = 3 biological replicates). (H) Following cell surface biotinylation and capture with streptavidin magnetic beads, Lrp1 and β3 integrin expression in the membrane fraction of wild-type and DKO osteoclasts as assessed by Western blot. Results are representative of three independent experiments. **P < 0.01. Statistical significance was assessed using one-way ANOVA with Bonferroni correction. Source data are available for this figure: SourceData F7.

Article Snippet: Antigen detection was performed using antibodies directed against c-Src (rabbit antimouse/human antibody; #2109; Cell Signaling), Ctsk (mouse anti-mouse/human antibody; sc-48353; Santa Cruz), Rho (mouse anti-mouse/human antibody; #05-778; Millipore), galectin-3 (mouse anti-mouse/human antibody; ab2785; Abcam; epitopes mapped within the N-terminal region), Lrp1 (mouse anti-mouse antibody; MABN1796; Millipore), Mmp9 (rabbit anti-mouse antibody; ab38898; Abcam), Mmp14 (rabbit anti-mouse antibody; ab53712; Abcam), OXPHOS (rabbit anti-mouse antibody; ab110413; Abcam), vinculin (mouse anti-mouse antibody; V9131; Sigma-Aldrich), β3 integrin (rabbit anti-mouse antibody; #4702; Cell Signaling), or β-actin (rabbit anti-mouse antibody; #4970; Cell Signaling).

Techniques: Control, Activation Assay, Incubation, Magnetic Beads, SDS Page, Mass Spectrometry, Binding Assay, Western Blot, Immunoprecipitation, Inhibition, Expressing, Membrane