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96
Proteintech anti gfp antibody
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Anti Gfp Antibody, supplied by Proteintech, 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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Rockland Immunochemicals chicken polyclonal anti gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Chicken Polyclonal Anti Gfp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Novus Biologicals nb100 1770ss rrid ab 10128178
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Nb100 1770ss Rrid Ab 10128178, supplied by Novus Biologicals, 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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94
Novus Biologicals goat anti gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Goat Anti Gfp, supplied by Novus Biologicals, 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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96
Santa Cruz Biotechnology mouse monoclonal anti gfp clone b2
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Mouse Monoclonal Anti Gfp Clone B2, 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/anti+gfp/GFP+Antibody/pm42879277-223-37-42
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ABclonal Biotechnology gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Gfp, supplied by ABclonal Biotechnology, 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/product/anti+gfp/Mouse+anti+GFP-Tag+mAb/pm42881188-440-6-7
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Santa Cruz Biotechnology gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Gfp, 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
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94
Synaptic Systems rabbit anti gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Rabbit Anti Gfp, supplied by Synaptic Systems, 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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Rockland Immunochemicals gfp rockland immunochemicals 600
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Gfp Rockland Immunochemicals 600, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gfp  (OriGene)
93
OriGene gfp
The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed <t>GFP-tagged</t> domains (green) in BmN4 cells. Representative merged bright-field and <t>GFP</t> fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with <t>an</t> <t>anti-GFP</t> antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.
Gfp, supplied by OriGene, 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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Image Search Results


The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed GFP-tagged domains (green) in BmN4 cells. Representative merged bright-field and GFP fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with an anti-GFP antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.

Journal: iScience

Article Title: Domain-autonomous MKLP1 modules divergently regulate mitotic fidelity and polyploidy in a holocentric system

doi: 10.1016/j.isci.2026.117149

Figure Lengend Snippet: The BmMKLP1 domains exhibit divergent nuclear and cytoplasmic localization (A) Subcellular localization of transiently expressed GFP-tagged domains (green) in BmN4 cells. Representative merged bright-field and GFP fluorescence images acquired at 10×, scale bars, 100 μm, BmN4 cells expressing the indicated constructs were imaged by differential interference contrast (DIC) microscopy (left) to show cell morphology and by fluorescence microscopy (right) to detect GFP-tagged proteins. All images were acquired with a 40× objective lens. Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with an anti-GFP antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight. The “control” lane corresponds to the cycle 3 GFP-bleo fusion protein (∼39–40 KDa) expressed from the pIZT/V5-His vector. A representative blot from three independent experiments is shown. The PageRuler Prestained Protein Ladder (10–180 kDa; Thermo Fisher Scientific, Waltham, MA, USA) was used as a molecular weight marker.

Article Snippet: Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with an anti-GFP antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight.

Techniques: Fluorescence, Expressing, Construct, Microscopy, Morphology, Western Blot, Analysis, Transfection, Molecular Weight, Control, Plasmid Preparation, Marker

The head and stalk domains induce G2/M arrest, whereas the tail promotes polyploidization (A) Representative flow cytometry histograms showing DNA content profiles (top) and polyploidy distributions (bottom) for control cells and cells expressing GFP-tagged BmMKLP1—full-length, head, -stalk, or -tail. Cell cycle phases (G0/G1, S, and G2/M) were determined by model-based fitting of propidium iodide (PI) fluorescence intensity histograms. Polyploidy histograms depict cells with DNA content exceeding 4 N. (B) Quantification of cell cycle distribution under each condition. Bars represent the mean ± SEM percentage of cells in G0/G1, S, and G2/M phases from at least three independent experiments. Different lowercase letters indicate significant differences (one-way ANOVA followed by Tukey’s HSD, p < 0.05). (C) Percentage of polyploid cells under each condition. Bars represent mean ± SEM, with statistical significance assessed as in (B).

Journal: iScience

Article Title: Domain-autonomous MKLP1 modules divergently regulate mitotic fidelity and polyploidy in a holocentric system

doi: 10.1016/j.isci.2026.117149

Figure Lengend Snippet: The head and stalk domains induce G2/M arrest, whereas the tail promotes polyploidization (A) Representative flow cytometry histograms showing DNA content profiles (top) and polyploidy distributions (bottom) for control cells and cells expressing GFP-tagged BmMKLP1—full-length, head, -stalk, or -tail. Cell cycle phases (G0/G1, S, and G2/M) were determined by model-based fitting of propidium iodide (PI) fluorescence intensity histograms. Polyploidy histograms depict cells with DNA content exceeding 4 N. (B) Quantification of cell cycle distribution under each condition. Bars represent the mean ± SEM percentage of cells in G0/G1, S, and G2/M phases from at least three independent experiments. Different lowercase letters indicate significant differences (one-way ANOVA followed by Tukey’s HSD, p < 0.05). (C) Percentage of polyploid cells under each condition. Bars represent mean ± SEM, with statistical significance assessed as in (B).

Article Snippet: Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with an anti-GFP antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight.

Techniques: Flow Cytometry, Control, Expressing, Fluorescence

Journal: iScience

Article Title: Domain-autonomous MKLP1 modules divergently regulate mitotic fidelity and polyploidy in a holocentric system

doi: 10.1016/j.isci.2026.117149

Figure Lengend Snippet:

Article Snippet: Scale bars, 20 μm. (B) Western blot analysis of protein extracts from transfected BmN4 cells probed with an anti-GFP antibody (1:1,000, Proteintech, Wuhan, China), confirming the production of each GFP-tagged domain at its expected molecular weight.

Techniques: Transfection, Cloning, Imaging, Bicinchoninic Acid Protein Assay, Western Blot, Plasmid Preparation, Recombinant, Software