anti rangap1 Search Results


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Rabbit Anti RANGAP1 Polyclonal Affinity Purified (PBS with 0.02% sodium azide, 50% glycerol, pH7.3) (Western Blot,IHC) from Innovative Research is a polyclonal antibody in a liquid format, buffered in PBS with 0.02% sodium azide, 50%
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90
Johns Hopkins HealthCare anti-rangap1 (19c7) mouse monoclonal antibody (mab)
(A) The diagram shows that compared to NPCs in the nuclear envelope, ALPCs are embedded in the membrane cisternae of annulate lamellae that are often connected to the membrane network of ER. (B) Human cervical cancer cells (HeLa) were double-labeled with anti-RanGAP1 antibody and <t>anti-SUMO1</t> mAb <t>(21C7)</t> or mAb414 for staining NPCs and ALPCs and then analyzed by immunofluorescence microscopy. (C) Mouse embryonic fibroblasts (NIH3T3) were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. (D) Rat primary cortical/hippocampal neurons (PN) were double-labeled with anti-RanGAP1 antibody and mAb414. (E) Human bronchial/tracheal smooth muscle cells (SMC) cells were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. Bar, 10 μm. The boxes at the top corner of each image show an enlarged version of inlets. (F) Annulate lamellae are highly abundant in SMC cells. 60 SMC cells were double-stained with anti-RanGAP1 antibody and mAb414. All the ALPC foci in each cell were counted under Olympus inverted IX81 fluorescence microscope using Z-stacks. The number of ALPC foci per cell was classified into three categories (10–50, 50–100 and ≥100), and the percentage of cells in each category was indicated. Each column represents the mean value ± SEM ( N = 60) (ALPC foci/cell: 10–182; Average = 63).
Anti Rangap1 (19c7) Mouse Monoclonal Antibody (Mab), supplied by Johns Hopkins HealthCare, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+rangap1/anti+rangap1++19c7++mouse+monoclonal+antibody++mab+/pmc04671610-34-14-25
Average 90 stars, based on 1 article reviews
anti-rangap1 (19c7) mouse monoclonal antibody (mab) - by Bioz Stars, 2026-10
90/100 stars
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90
ZenBio rabbit monoclonal anti-rangap1 (cat. no. r383099)
The new SUMO E1 CAIs perturb the SUMOylation pathway. T47D cells were treated with MCULE-3064932370 and MCULE-6830015021 for 48 h before evaluation. (a) The cellular levels of <t>RanGAP1,</t> RanGAP1-SUMO, and SUMO1 were assessed by Western blotting. (b) The cellular levels of Uba2 and Ubc9 were assessed by Western blotting.
Rabbit Monoclonal Anti Rangap1 (Cat. No. R383099), supplied by ZenBio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+rangap1/rabbit+monoclonal+anti+RanGAP1++Cat++NO++R383099/bio_rxiv__2024__12__12__627095-152-1-15
Average 90 stars, based on 1 article reviews
rabbit monoclonal anti-rangap1 (cat. no. r383099) - by Bioz Stars, 2026-10
90/100 stars
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Boster Bio Anti-RANGAP1 Antibody Picoband® catalog # A02771-2. Tested in ELISA, Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that
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Boster Bio Anti-RANGAP1 mouse monoclonal antibody, clone OTI1B4 (formerly 1B4). Catalog# M02771. Tested in FC, IF, IHC, WB. This antibody reacts with Human, Mouse, Rat, Dog.
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RANGAP1 Polyclonal Antibody
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This gene encodes a protein that associates with the nuclear pore complex and participates in the regulation of nuclear transport. The encoded protein interacts with Ras-related nuclear protein 1 (RAN) and regulates guanosine triphosphate (GTP)-binding
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Boster Bio Anti-RanGAP1 Antibody catalog # A02771-1. Tested in WB,ICC,IF,IHC,Flow Cytometry,IP applications. This antibody reacts with Human,Mouse,Rat.
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Rabbit Anti Human RANGAP1 Polyclonal Affinity Purified (PBS with 0.02% sodium azide, 50% glycerol, pH7.3) (Immunofluorescence) from Innovative Research is a polyclonal antibody in a liquid format, buffered in PBS with 0.02% sodium azide, 50%
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Image Search Results


(A) The diagram shows that compared to NPCs in the nuclear envelope, ALPCs are embedded in the membrane cisternae of annulate lamellae that are often connected to the membrane network of ER. (B) Human cervical cancer cells (HeLa) were double-labeled with anti-RanGAP1 antibody and anti-SUMO1 mAb (21C7) or mAb414 for staining NPCs and ALPCs and then analyzed by immunofluorescence microscopy. (C) Mouse embryonic fibroblasts (NIH3T3) were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. (D) Rat primary cortical/hippocampal neurons (PN) were double-labeled with anti-RanGAP1 antibody and mAb414. (E) Human bronchial/tracheal smooth muscle cells (SMC) cells were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. Bar, 10 μm. The boxes at the top corner of each image show an enlarged version of inlets. (F) Annulate lamellae are highly abundant in SMC cells. 60 SMC cells were double-stained with anti-RanGAP1 antibody and mAb414. All the ALPC foci in each cell were counted under Olympus inverted IX81 fluorescence microscope using Z-stacks. The number of ALPC foci per cell was classified into three categories (10–50, 50–100 and ≥100), and the percentage of cells in each category was indicated. Each column represents the mean value ± SEM ( N = 60) (ALPC foci/cell: 10–182; Average = 63).

Journal: PLoS ONE

Article Title: Molecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells

doi: 10.1371/journal.pone.0144508

Figure Lengend Snippet: (A) The diagram shows that compared to NPCs in the nuclear envelope, ALPCs are embedded in the membrane cisternae of annulate lamellae that are often connected to the membrane network of ER. (B) Human cervical cancer cells (HeLa) were double-labeled with anti-RanGAP1 antibody and anti-SUMO1 mAb (21C7) or mAb414 for staining NPCs and ALPCs and then analyzed by immunofluorescence microscopy. (C) Mouse embryonic fibroblasts (NIH3T3) were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. (D) Rat primary cortical/hippocampal neurons (PN) were double-labeled with anti-RanGAP1 antibody and mAb414. (E) Human bronchial/tracheal smooth muscle cells (SMC) cells were double-stained with anti-RanGAP1 antibody and mAb414 or anti-RanBP2 mAb. Bar, 10 μm. The boxes at the top corner of each image show an enlarged version of inlets. (F) Annulate lamellae are highly abundant in SMC cells. 60 SMC cells were double-stained with anti-RanGAP1 antibody and mAb414. All the ALPC foci in each cell were counted under Olympus inverted IX81 fluorescence microscope using Z-stacks. The number of ALPC foci per cell was classified into three categories (10–50, 50–100 and ≥100), and the percentage of cells in each category was indicated. Each column represents the mean value ± SEM ( N = 60) (ALPC foci/cell: 10–182; Average = 63).

Article Snippet: Antibodies used in this study were obtained from the following sources: anti-RanGAP1 (19C7) and anti-SUMO1 (21C7) mouse monoclonal antibodies (mAbs) [ ], Dr. Michael Matunis (Johns Hopkins, Baltimore, MD); anti-RanGAP1 rabbit polyclonal antibody (pAb) [ ], Dr. Mary Dasso (NIH, Bethesda, MD); anti-POM121 rabbit pAb (EMD Millipore); anti-tubulin mouse mAb (Sigma); anti-Myc (9E10) mAb (Santa Cruz); anti-lamin B goat pAb (Santa Cruz); anti-nucleophosmin rabbit pAb (Santa Cruz); anti-RanBP2 mouse mAb (Santa Cruz); anti-RanBP2 rabbit pAb (Abcam); mAb414 mouse mAb (Covance); anti-Myc rabbit pAb (Cell Signaling); anti-calreticulin rabbit pAb (Calbiochem); anti-ELYS mouse mAb (Bio Matrix Research); anti-ELYS rabbit pAb (Bethyl Laboratories); anti-importin α mouse mAb (BD Biosciences); anti-importin β mouse mAb (BD Biosciences); anti-CRM1 mouse mAbs (BD Biosciences; Santa Cruz); anti-FLAG mouse mAb (M2) (Sigma); anti-FLAG rabbit pAb (Sigma); anti-Ubc9 rabbit pAb (Abcam); anti-Ran mouse mAb (BD Biosciences).

Techniques: Membrane, Labeling, Staining, Immunofluorescence, Microscopy, Fluorescence

(A-D) HeLa cells were double stained with mAb414 and calreticulin antibody for labeling ER network (A), mAb414 and RanBP2 antibody (B), tubulin and calreticulin antibodies (C), and tubulin and RanBP2 antibodies (D) followed by immunofluorescence microscopy. The enlarged versions of inlets are shown at the bottom or top corner of each image (A-D). The arrows indicate the positions of the ALPC-associated RanBP2/RanGAP1*SUMO1/Ubc9 complexes that are most distant from the corresponding nucleus (D). The immunofluorescent images were taken using Olympus inverted IX81 widefield fluorescence microscope with U-Plan S-Apo 60×/1.35 NA oil immersion objective. Bar, 10 μm.

Journal: PLoS ONE

Article Title: Molecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells

doi: 10.1371/journal.pone.0144508

Figure Lengend Snippet: (A-D) HeLa cells were double stained with mAb414 and calreticulin antibody for labeling ER network (A), mAb414 and RanBP2 antibody (B), tubulin and calreticulin antibodies (C), and tubulin and RanBP2 antibodies (D) followed by immunofluorescence microscopy. The enlarged versions of inlets are shown at the bottom or top corner of each image (A-D). The arrows indicate the positions of the ALPC-associated RanBP2/RanGAP1*SUMO1/Ubc9 complexes that are most distant from the corresponding nucleus (D). The immunofluorescent images were taken using Olympus inverted IX81 widefield fluorescence microscope with U-Plan S-Apo 60×/1.35 NA oil immersion objective. Bar, 10 μm.

Article Snippet: Antibodies used in this study were obtained from the following sources: anti-RanGAP1 (19C7) and anti-SUMO1 (21C7) mouse monoclonal antibodies (mAbs) [ ], Dr. Michael Matunis (Johns Hopkins, Baltimore, MD); anti-RanGAP1 rabbit polyclonal antibody (pAb) [ ], Dr. Mary Dasso (NIH, Bethesda, MD); anti-POM121 rabbit pAb (EMD Millipore); anti-tubulin mouse mAb (Sigma); anti-Myc (9E10) mAb (Santa Cruz); anti-lamin B goat pAb (Santa Cruz); anti-nucleophosmin rabbit pAb (Santa Cruz); anti-RanBP2 mouse mAb (Santa Cruz); anti-RanBP2 rabbit pAb (Abcam); mAb414 mouse mAb (Covance); anti-Myc rabbit pAb (Cell Signaling); anti-calreticulin rabbit pAb (Calbiochem); anti-ELYS mouse mAb (Bio Matrix Research); anti-ELYS rabbit pAb (Bethyl Laboratories); anti-importin α mouse mAb (BD Biosciences); anti-importin β mouse mAb (BD Biosciences); anti-CRM1 mouse mAbs (BD Biosciences; Santa Cruz); anti-FLAG mouse mAb (M2) (Sigma); anti-FLAG rabbit pAb (Sigma); anti-Ubc9 rabbit pAb (Abcam); anti-Ran mouse mAb (BD Biosciences).

Techniques: Staining, Labeling, Immunofluorescence, Microscopy, Fluorescence

ALPCs may serve as the docking or assembling sites for importin α/β-mediated import complexes followed by their dissociation for nuclear import. On the other hand, the ALPC-associated RanBP2/RanGAP1*SUMO1/Ubc9 complexes may function in the disassembly of CRM1-mediated export complexes by mediating RanGTP hydrolysis.

Journal: PLoS ONE

Article Title: Molecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells

doi: 10.1371/journal.pone.0144508

Figure Lengend Snippet: ALPCs may serve as the docking or assembling sites for importin α/β-mediated import complexes followed by their dissociation for nuclear import. On the other hand, the ALPC-associated RanBP2/RanGAP1*SUMO1/Ubc9 complexes may function in the disassembly of CRM1-mediated export complexes by mediating RanGTP hydrolysis.

Article Snippet: Antibodies used in this study were obtained from the following sources: anti-RanGAP1 (19C7) and anti-SUMO1 (21C7) mouse monoclonal antibodies (mAbs) [ ], Dr. Michael Matunis (Johns Hopkins, Baltimore, MD); anti-RanGAP1 rabbit polyclonal antibody (pAb) [ ], Dr. Mary Dasso (NIH, Bethesda, MD); anti-POM121 rabbit pAb (EMD Millipore); anti-tubulin mouse mAb (Sigma); anti-Myc (9E10) mAb (Santa Cruz); anti-lamin B goat pAb (Santa Cruz); anti-nucleophosmin rabbit pAb (Santa Cruz); anti-RanBP2 mouse mAb (Santa Cruz); anti-RanBP2 rabbit pAb (Abcam); mAb414 mouse mAb (Covance); anti-Myc rabbit pAb (Cell Signaling); anti-calreticulin rabbit pAb (Calbiochem); anti-ELYS mouse mAb (Bio Matrix Research); anti-ELYS rabbit pAb (Bethyl Laboratories); anti-importin α mouse mAb (BD Biosciences); anti-importin β mouse mAb (BD Biosciences); anti-CRM1 mouse mAbs (BD Biosciences; Santa Cruz); anti-FLAG mouse mAb (M2) (Sigma); anti-FLAG rabbit pAb (Sigma); anti-Ubc9 rabbit pAb (Abcam); anti-Ran mouse mAb (BD Biosciences).

Techniques:

The new SUMO E1 CAIs perturb the SUMOylation pathway. T47D cells were treated with MCULE-3064932370 and MCULE-6830015021 for 48 h before evaluation. (a) The cellular levels of RanGAP1, RanGAP1-SUMO, and SUMO1 were assessed by Western blotting. (b) The cellular levels of Uba2 and Ubc9 were assessed by Western blotting.

Journal: bioRxiv

Article Title: SUMO E1 covalent allosteric inhibitors modulate polyamine synthesis via the MAT2A-AdoMetDC axis

doi: 10.1101/2024.12.12.627095

Figure Lengend Snippet: The new SUMO E1 CAIs perturb the SUMOylation pathway. T47D cells were treated with MCULE-3064932370 and MCULE-6830015021 for 48 h before evaluation. (a) The cellular levels of RanGAP1, RanGAP1-SUMO, and SUMO1 were assessed by Western blotting. (b) The cellular levels of Uba2 and Ubc9 were assessed by Western blotting.

Article Snippet: The rabbit monoclonal anti-RanGAP1 (Cat. NO. R383099) and anti-MAT2A (Cat. NO. R389369) antibodies were from ZenBio, Inc. (U.S.A.).

Techniques: Western Blot