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anti gfp antibody  (Proteintech)


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    Structured Review

    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 1652 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/gfp/GFP+tag+Antibody/pmc13657243-107-18-21
    Average 96 stars, based on 1652 article reviews
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    Images

    1) Product Images from "Domain-autonomous MKLP1 modules divergently regulate mitotic fidelity and polyploidy in a holocentric system"

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

    Journal: iScience

    doi: 10.1016/j.isci.2026.117149

    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.
    Figure Legend 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.

    Techniques Used: 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).
    Figure Legend 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).

    Techniques Used: Flow Cytometry, Control, Expressing, Fluorescence


    Figure Legend Snippet:

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

    Related Articles

    Incubation:

    Article Title: Spatiotemporal coordination of Slit-Robo repulsion and neurturin-Gfrα attraction guides multipolar migration during retinal lamination
    Article Snippet: .. Following primary antibodies, incubated for 72 h at 4°C, were used in the study 1:200 GFP (50430-2-AP, Proteintech), 1:800 HuC/D (A-21271 Invitrogen) 1:500 Zpr-1 (AB_10013803, Zirc), 1:800 Prox1 (AB5475, Sigma Aldrich), 1:50 Robo2 (45568, Cell Signaling, 90% epitope identity to zebrafish Robo2). .. All primary antibodies were diluted in 1% goat serum in PBS-T. Primary antibody incubation was followed by 5 × 30 min washes with PBS-T and 48-h incubation at 4°C with Alexa Fluor 488 goat anti-rabbit (A-11034, Invitrogen), Alexa Fluor 647 goat anti-rabbit (A-21245, Invitrogen) or Alexa Fluor 647 goat anti-mouse (A-21236, Invitrogen).

    Article Title: Ribbon-shaped microgels as bioinks for 3D bioprinting of anisotropic tissue structures
    Article Snippet: .. Primary antibody for osteocalcin (1:200, 23418-1-AP, Proteintech), GFP (1:100, 50430-2-AP, Proteintech) was diluted in 1 % BSA with 0.1 % Triton X-100 and incubated overnight at 4 °C. .. After 3 washes with PBS, slides were incubated with secondary antibody, goat anti-rabbit IgG AlexaFluor 647 (1:500, A-21245, Invitrogen), goat anti-rabbit IgG AlexaFluor 488 (1:500, A32731, Invitrogen) for 1 h at room temperature.

    Plasmid Preparation:

    Article Title: VAMP7-dependent late endosomal secretion of ER and mitochondrial proteins impacts the tumor microenvironment and macrophage engagement.
    Article Snippet: Starvation was induced by replacing cell medium with EBSS (ThermoFisher, 24010043) supplemented with 0.2% BSA for 2 hours at 37°C and 5% CO2, followed, in the refeeding condition, by refeeding the cells with full cell medium for 30 minutes. .. Plasmids used in the study were as follows: pEGFP-C3 (Clonetech Technologies), GFP-VAMP7, RFPLongin (described in 80), pcDNA3.1-Myc-His RTN3A1 was a gift from Jimtong Horng (Addgene plasmid # 31087; http://n2t.net/addgene:31087 ; RRID:Addgene_31087), GFP-CD63 was a gift from John Paul Luzio (Cambridge), Flag-RTN3L was a gift from Ivan Dikic 44, ptfLC3 was a gift from Tamotsu Yoshimori (Addgene plasmid # 21074 ; http://n2t.net/addgene:21074 ; RRID:Addgene_21074). .. Primary and secondary antibodies used in the study were as follows: Anti RTN3 (Abcam, ab187764, Western blotting [WB] 1/1000, Immunoflouorescence [IF] 1/250), Anti CD63 (BD Pharmingen, 551458, WB 1/1000, IF 1/250), Anti VDAC1/2 (Proteintech, 55259-1-AP, Abcam, ab14734, WB 1/2000), Anti Myc (Cell Signaling, 2272S, WB 1/1000) Anti Tubulin (Proteintech, 10094-1- AP, WB 1/5000), Anti GFP (Proteintech, 50430-2-AP, WB 1/4000), Anti SNAP47 (SYSY, 111403, WB 1/1000), Anti Syntaxin5 (Gift from Richard Scheller, WB 1/1000), Anti Syntaxin17 (Sigma-Aldrich, HPA001204, WB 1/1000), Anti GRP78/Bip (Proteintech, 11587-1-AP, WB 1/2000), Anti Phospho-eIF2α (Ser51) (Cell Signaling, D9G8, WB 1/1000), Total eIF2α (Cell Signaling, D7D3, WB 1/1000), GAPDH (Sigma-Aldrich, G9545, WB 1/10000), Anti p-S616 DRP1 (Cell Signaling, 4494S, WB 1/1000), Anti p- AR TI CL E IN P RE SS S637 DRP1 (Cell Signaling, 6319, WB 1/1000), Anti DRP1 (Cell Signaling, 8570S, WB 1/1000), Anti MFF (Cell Signaling, 84580 WB 1/1000), Anti OPA1 (BD Biosciences, 612606, WB 1/1000), Anti MFN2 (Abcam, ab124773, WB 1/1000), Anti Beta-Actin (Sigma-Aldrich, A5441, WB 1/20000), Anti pS2448mTOR (Cell Signaling, 5536P, WB 1/1000), Anti mTOR (Cell Signaling, 2983P, WB 1/1000), Anti LC3B (Abcam, ab48394, WB 1/1000), Anti p62/SQSTM1 (Abcam, ab56416, WB 1/5000), Anti pS757-ULK1 (Cell Signaling, 14202T, WB 1/1000), Anti ULK1 (Cell Signaling, 8054, WB 1/1000), Anti pT389-P70S6K (Cell Signaling, 9208S, WB 1/1000), P70S6K (Cell Signaling, 9234, WB 1/1000), Anti-rabbit IgG, HRPlinked Antibody (Cell Signaling, 7074, WB 1/10000), Anti-Mouse IgG, HRP- linked Antibody (Cell Signaling, 7076, WB 1/10000), Alexa Fluor 568 Goat Anti-Mouse (ThermoScientific, A11031, IF 1/250), Alexa Fluor 568 Donkey Anti-Mouse (ThermoScientific, A10037, IF 1/250), Alexa Fluor 488 Donkey Anti- Rabbit (ThermoScientific, A21206, IF 1/250), Vimentin (Abcam ab92547, EPR3776, IHC 1/250), Iba1 (WAKO, 019-19741, IHC 1/800).

    Chromatin Immunoprecipitation:

    Article Title: A proteome-wide dependency map of protein interaction motifs.
    Article Snippet: Short linear motifs (SLiMs) are the most ubiquitous protein interaction motifs within unstructured regions of the human proteome, yet their contribution to cellular homeostasis remains poorly understood.. Here, to systematically assess SLiM function, we applied base editing to mutate all reported and a set of computationally predicted SLiMs defined by SLiM-like evolutionary patterns.. By screening 7,293 SLiM-containing regions with 80,473 mutations in HAP1 cells, we define a SLiM dependency map identifying 450 reported and 264 predicted SLiMs required for normal cell proliferation.

    Flow Cytometry:

    Article Title: A proteome-wide dependency map of protein interaction motifs.
    Article Snippet: Short linear motifs (SLiMs) are the most ubiquitous protein interaction motifs within unstructured regions of the human proteome, yet their contribution to cellular homeostasis remains poorly understood.. Here, to systematically assess SLiM function, we applied base editing to mutate all reported and a set of computationally predicted SLiMs defined by SLiM-like evolutionary patterns.. By screening 7,293 SLiM-containing regions with 80,473 mutations in HAP1 cells, we define a SLiM dependency map identifying 450 reported and 264 predicted SLiMs required for normal cell proliferation.

    Magnetic Resonance Imaging:

    Article Title: A proteome-wide dependency map of protein interaction motifs.
    Article Snippet: Short linear motifs (SLiMs) are the most ubiquitous protein interaction motifs within unstructured regions of the human proteome, yet their contribution to cellular homeostasis remains poorly understood.. Here, to systematically assess SLiM function, we applied base editing to mutate all reported and a set of computationally predicted SLiMs defined by SLiM-like evolutionary patterns.. By screening 7,293 SLiM-containing regions with 80,473 mutations in HAP1 cells, we define a SLiM dependency map identifying 450 reported and 264 predicted SLiMs required for normal cell proliferation.

    other:

    Article Title: MCOLN1-mediated PPP3CB activation alleviates neuronal damage by promoting TFEB-dependent autophagic flux in permanent cerebral ischemia
    Article Snippet: We previously reported that transcription factor EB (TFEB) plays a crucial role in regulating the ischemic stroke (IS)-mediated dynamic changes of autophagic flux.. Protein phosphatase 3 (PPP3) may regulate the transcriptional activity of TFEB.. However, the main isoform of the PPP3 catalytic subunit (PPP3C) involved in TFEB activation, the PPP3-binding site in TFEB, and the upstream regulatory mechanism of PPP3 activation after cerebral ischemia are still unknown.

    Staining:

    Article Title: Spatiotemporal coordination of Slit-Robo repulsion and neurturin-Gfrα attraction guides multipolar migration during retinal lamination
    Article Snippet: .. Tg(lhx1:GFP) or Tg(ptf1a:Gal4; UAS:gap-YFP) embryos grown to 52- and 54 hpf in the presence of 0.2 mM PTU, were fixed overnight at 4°C with 4% PFA and expanded using an adapted UltraExM protocol based on., , , Prior expansion, the Tg(ptf1a:Gal4; UAS:gap-YFP) embryos were stained with 1:200 GFP (50430-2-AP, Proteintech) whereas the Tg(lhx1:GFP) embryos were processed straight for expansion. .. The embryos were washed 3 × 15 min with PBS-T and incubated overnight at RT in linking solution (0.1 mg/mL acryloyl X-SE (Invitrogen, A20770) in 0.1% PBS-T).



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    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