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rabbit polyclonal anti map1b antibody (Proteintech)

Name: rabbit polyclonal anti map1b antibody
Brand: Proteintech
Rating: 93 (17 reviews)

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Proteintech rabbit polyclonal anti map1b antibody

Figure 4. BFSP1 interacts with <t>MAP1B</t> 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.

Rabbit Polyclonal Anti Map1b Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 17 article reviews

rabbit polyclonal anti map1b antibody - by Bioz Stars, 2026-02

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1) Product Images from "Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length."

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

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

doi: 10.1002/advs.202504066

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.

Figure Legend 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.

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

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.

Figure Legend 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.

Techniques Used: Control

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

Figure Legend 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

Techniques Used: Control, Microinjection

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.

Figure Legend 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.

Techniques Used: Co-Immunoprecipitation Assay, Western Blot, Control

Image Search Results

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.

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

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.

Techniques: Co-Immunoprecipitation Assay, Western Blot, Control

Journal: Journal of Orthopaedic Surgery and Research

Article Title: Electroacupuncture attenuates intervertebral disc degeneration by upregulating aquaporins via the cAMP/PKA pathway

doi: 10.1186/s13018-025-05729-9

Figure Lengend Snippet: Antibody Dilution ratio

Article Snippet: rabbit anti-MAP1B , DF12422 , 1:1000 , Affinity Biosciences, China.

Techniques:

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

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1) Product Images from "Intermediate Filament Protein BFSP1 Maintains Oocyte Asymmetric Division by Modulating Spindle Length."

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