map1b polyclonal antibody  (Proteintech)

Journal: Frontiers in Oncology

Article Title: CDK1-driven phosphorylation networks promote glioblastoma progression via MAP1B-mediated microtubule destabilization

doi: 10.3389/fonc.2025.1646698

Figure Lengend Snippet: CDK1-mediated MAP1B phosphorylation is positively correlated with the prognosis of GBM. (A) Overlap analysis of CPTAC phosphoproteome data (blue) with CDK1-regulated phosphosites (red). (B) Heatmap of MAP1B phosphosites in the shCDK1 and shCtrl groups. Red indicates upregulated values relative to the mean, while blue indicates downregulated values relative to the mean. The intensity of the color corresponds to the magnitude of the deviation. (C) Prognostic significance of MAP1B phosphorylation sites. Kaplan-Meier survival analysis of GBM patients stratified by phosphorylation levels at S832, S1260, S1899, S1939, S2209, S2271(log-rank test, p < 0.05). High phosphorylation correlates with poor overall survival (n=99). (D, E) CoIP showing interactions between CDK1 and MAP1B. (F) Detecting pS/T phosphorylation of MAP1B in shCDK1 and shCtrl U251 cells. (G) Detecting pS/T phosphorylation of MAP1B in overexpressed-CDK1(OE-CDK1) and empty vector(Vector) U251 cells.

Article Snippet: Phospho-(Ser/Thr) Phe Antibody (#9631, Cell Signaling Technology), MAP1B Polyclonal antibody(21633-1-AP, proteintech) and β-actin Polyclonal antibody(20536-1-AP, proteintech) were used for western blot.

Techniques: Phospho-proteomics, Plasmid Preparation

Journal: Frontiers in Oncology

Article Title: CDK1-driven phosphorylation networks promote glioblastoma progression via MAP1B-mediated microtubule destabilization

doi: 10.3389/fonc.2025.1646698

Figure Lengend Snippet: CDK1-mediated phosphorylation of MAP1B regulates microtubule stability in U251 cells. (A) Wound healing assays showing delayed gap closure in shMAP1B cells compared to shCtrl cells over 36 hours, ***p < 0.001 (t-test), ****p < 0.0001 (t-test). (B) Transwell migration assays confirmed the impaired migration ability of shMAP1B cells. ***p < 0.001 (t-test). (C) CCK-8 proliferation assays revealed a significant decrease in cell viability in shMAP1B cells ***p < 0.001 (t-test). (D) Wiki-pathways analysis of differently expressed phosphoproteins. (E) Representative photographs of alpha tubulin staining of in U251 cells. Scale bar: 20 μm. Cells were stained with an antibody against acetyl-α-tubulin (green). Nuclei were counterstained with DAPI (blue). Scale bar, 20 μm.

Article Snippet: Phospho-(Ser/Thr) Phe Antibody (#9631, Cell Signaling Technology), MAP1B Polyclonal antibody(21633-1-AP, proteintech) and β-actin Polyclonal antibody(20536-1-AP, proteintech) were used for western blot.

Techniques: Phospho-proteomics, Migration, CCK-8 Assay, Staining

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length.

doi: 10.1002/advs.202504066

Figure Lengend Snippet: Figure 4. BFSP1 interacts with MAP1B and affects its protein stability. A) Identification of BFSP1 binding proteins by IP/MS analysis. Protein name, cov- erage percentage, the number of identified peptides, and molecular weight were shown in the table. B) Representation of the 3D structure and predicted interaction of mouse BFSP1 and MAP1B using AlphaFold databank by HDOCK server. C) Co-IP using anti-BFSP1 antibody followed by immunoblotting analysis with anti-MAP1B and anti-BFSP1 antibodies. D) Co-IP using anti-MAP1B antibody followed by immunoblotting analysis with anti-BFSP1 and anti-MAP1B antibodies. E) Representative images of MAP1B in control and BFSP1-KD oocytes. Scale bar, 10 μm. F) The ratio of MAP1B fluorescence intensity in the spindle region to the cytoplasmic region was measured in control and BFSP1-KD oocytes. G) Protein levels of MAP1B in control, BFSP1- KD, and BFSP1-rescue oocytes as assessed by immunoblotting analysis. The band intensity of BFSP1 and MAP1B was normalized with that of GAPDH. H) The band intensities of BFSP1 and MAP1B in the blots were normalized with that of GAPDH. Data in (F) were expressed as mean ± SD, and (H) were expressed as mean ± SEM of at least three independent experiments. ***P < 0.001; ns, no significance.

Article Snippet: Antibodies: Rabbit polyclonal anti-BFSP1 antibody (Cat# A3764) and rabbit monoclonal anti-Myc antibody (Cat# AE070) were purchased fromAbclonal (Wuhan, China); rabbit polyclonal anti-MAP1B antibody (Cat# 21633-1-AP), rabbit polyclonal antiHSP90α antibody (Cat# 13171-1-AP), mouse monoclonal anti-βActin antibody (Cat# 66009-1-lg), rabbit polyclonal anti-HA antibody (Cat# 51064-2-AP), and mouse monoclonal anti-GAPDH antibody (Cat# 60004-1-lg) were purchased from Proteintech (Rosemont, IL, USA); mouse monoclonal anti-α-Tubulin-FITC antibody (Cat# F2168) was purchased from Sigma–Aldrich (St. Louis, MO, USA); rabbit monoclonal anti-Vinculin antibody (Cat# CY5164) was purchased from Always (Shanghai, China).

Techniques: Binding Assay, Protein-Protein interactions, Molecular Weight, Co-Immunoprecipitation Assay, Western Blot, Control

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length.

doi: 10.1002/advs.202504066

Figure Lengend Snippet: Figure 5. MAP1B depletion impairs the oocyte meiotic maturation and spindle length control. A) Representative images of oocytes at M II stage in control and MAP1B-KD groups. Yellow asterisks indicate oocytes that failed to extrude the first polar body, and red asterisks indicate oocytes with symmetric division. Scale bar, 80 μm. B) The GVBD rate was quantified in control (n = 202) and MAP1B-KD (n = 189) oocytes. C) The PBE rate was quantified in control (n = 202) and MAP1B-KD (n = 189) oocytes. D) The rate of symmetric division was quantified in control (n = 202) and MAP1B-KD (n = 189) oocytes. E) Representative images of spindle length in control and MAP1B-KD oocytes at M I stage. Oocytes were immunostained for 𝛼-tubulin and 𝛾-tubulin. Scale bar, 15 μm. F) Spindle length was measured between two spindle poles in control (n = 23) and MAP1B-KD (n = 26) oocytes at M I stage. G) Representative images of spindle length in control and MAP1B-KD oocytes at AT I stage. Oocytes were immunostained for 𝛼-tubulin and 𝛾-tubulin. Scale bar, 15 μm. H) Spindle length was measured between two spindle poles in control (n = 15) and MAP1B-KD (n = 19) oocytes at AT I stage. Data in (B), (C), and (D) were expressed as mean ± SEM, and (F) and (H) were expressed as mean ± SD of at least three independent experiments. *P < 0.05; **P < 0.01; ***P < 0.001.

Article Snippet: Antibodies: Rabbit polyclonal anti-BFSP1 antibody (Cat# A3764) and rabbit monoclonal anti-Myc antibody (Cat# AE070) were purchased fromAbclonal (Wuhan, China); rabbit polyclonal anti-MAP1B antibody (Cat# 21633-1-AP), rabbit polyclonal antiHSP90α antibody (Cat# 13171-1-AP), mouse monoclonal anti-βActin antibody (Cat# 66009-1-lg), rabbit polyclonal anti-HA antibody (Cat# 51064-2-AP), and mouse monoclonal anti-GAPDH antibody (Cat# 60004-1-lg) were purchased from Proteintech (Rosemont, IL, USA); mouse monoclonal anti-α-Tubulin-FITC antibody (Cat# F2168) was purchased from Sigma–Aldrich (St. Louis, MO, USA); rabbit monoclonal anti-Vinculin antibody (Cat# CY5164) was purchased from Always (Shanghai, China).

Techniques: Control

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length.

doi: 10.1002/advs.202504066

Figure Lengend Snippet: Figure 6. Restored MAP1B protein levels mitigate the meiotic defects in- duced in BFSP1 depleted-oocytes. A) Representative images of oocytes at M II stage in control, BFSP1-KD, and MAP1B-rescue groups. For the res- cue experiment, MAP1B-EGFP mRNA was microinjected to GV oocytes 20 h after microinjection of BFSP1 siRNAs. Yellow asterisks indicate oocytes that failed to extrude the first polar body, and red asterisks indicate oocytes with symmetric division. Scale bar, 80 μm. B) The GVBD rate was quan- tified in control (n = 180), BFSP1-KD (n = 174), and MAP1B-rescue (n = 185) oocytes. C) The PBE rate was quantified in control (n = 180), BFSP1- KD (n = 174), and MAP1B-rescue (n = 185) oocytes. D) The rate of sym- metric division was quantified in control (n = 180), BFSP1-KD (n = 174), and MAP1B-rescue (n = 185) oocytes. E) Representative images of spin- dle length in control, BFSP1-KD, and MAP1B-rescue oocytes at M I stage. Oocytes were immunostained for 𝛼-tubulin and 𝛾-tubulin. Scale bar, 15 μm. F) Spindle length was measured between two spindle poles in control (n = 19), BFSP1-KD (n = 19), and MAP1B-rescue (n = 14) oocytes at M I stage. G) Representative images of spindle length in control, BFSP1-KD, and MAP1B-rescue oocytes at AT I stage. Oocytes were immunostained

Article Snippet: Antibodies: Rabbit polyclonal anti-BFSP1 antibody (Cat# A3764) and rabbit monoclonal anti-Myc antibody (Cat# AE070) were purchased fromAbclonal (Wuhan, China); rabbit polyclonal anti-MAP1B antibody (Cat# 21633-1-AP), rabbit polyclonal antiHSP90α antibody (Cat# 13171-1-AP), mouse monoclonal anti-βActin antibody (Cat# 66009-1-lg), rabbit polyclonal anti-HA antibody (Cat# 51064-2-AP), and mouse monoclonal anti-GAPDH antibody (Cat# 60004-1-lg) were purchased from Proteintech (Rosemont, IL, USA); mouse monoclonal anti-α-Tubulin-FITC antibody (Cat# F2168) was purchased from Sigma–Aldrich (St. Louis, MO, USA); rabbit monoclonal anti-Vinculin antibody (Cat# CY5164) was purchased from Always (Shanghai, China).

Techniques: Control, Microinjection

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length.

doi: 10.1002/advs.202504066

Figure Lengend Snippet: Figure 7. BFSP1 maintains MAP1B protein levels by recruiting HSP90𝛼. A) Co-IP using anti-BFSP1 antibody followed by immunoblotting analysis with anti-HSP90𝛼and anti-BFSP1 antibodies. B) Protein levels of MAP1B in control and 17-AAG-treated oocytes as assessed by immunoblotting analysis. C) The band intensity of MAP1B in the blots was normalized with that of 𝛽-Actin. D) Protein levels of HSP90𝛼in control and BFSP1-KD oocytes as assessed by immunoblotting analysis. E) The band intensities of BFSP1 and HSP90𝛼in the blots were normalized with that of 𝛽-Actin. F) Representative images of HSP90𝛼localization in the spindle region in control and BFSP1-KD oocytes. Scale bars, 20 μm, 10 μm. Data in (C) and (E) were expressed as mean ± SEM of at least three independent experiments. ***P < 0.001; ns, no significance.

Article Snippet: Antibodies: Rabbit polyclonal anti-BFSP1 antibody (Cat# A3764) and rabbit monoclonal anti-Myc antibody (Cat# AE070) were purchased fromAbclonal (Wuhan, China); rabbit polyclonal anti-MAP1B antibody (Cat# 21633-1-AP), rabbit polyclonal antiHSP90α antibody (Cat# 13171-1-AP), mouse monoclonal anti-βActin antibody (Cat# 66009-1-lg), rabbit polyclonal anti-HA antibody (Cat# 51064-2-AP), and mouse monoclonal anti-GAPDH antibody (Cat# 60004-1-lg) were purchased from Proteintech (Rosemont, IL, USA); mouse monoclonal anti-α-Tubulin-FITC antibody (Cat# F2168) was purchased from Sigma–Aldrich (St. Louis, MO, USA); rabbit monoclonal anti-Vinculin antibody (Cat# CY5164) was purchased from Always (Shanghai, China).

Techniques: Co-Immunoprecipitation Assay, Western Blot, Control

Journal: iScience

Article Title: Single-cell atlas unveils cellular heterogeneity and novel markers in human neonatal and adult intervertebral discs

doi: 10.1016/j.isci.2022.104504

Figure Lengend Snippet:

Article Snippet: Rabbit Polyclonal Anti-MAP1B , Novus Biologicals , NBP3-04801-20ul.

Techniques: Recombinant, Gene Expression, Software