Chicken α gfp

Manufactured by Abcam

Sourced in Japan

Chicken α-GFP is an antibody that specifically recognizes and binds to the green fluorescent protein (GFP) derived from the jellyfish Aequorea victoria. This antibody can be used to detect and visualize GFP-tagged proteins in various experimental applications.

Automatically generated - may contain errors

Lab products found in correlation

Mouse α tubulin, by Merck Group (2 mentions) Rabbit α rfp, by Rockland Immunochemicals (2 mentions) Mouse α gs, by Merck Group (2 mentions) Alexa 488 α chicken, by Jackson ImmunoResearch (2 mentions) Rhodamine red x α rabbit, by Jackson ImmunoResearch (2 mentions) Dylight 649 α mouse, by Vector Laboratories (2 mentions) Vectashield antifade mounting medium, by Vector Laboratories (2 mentions) Goat α chicken alexa fluor 488, by Thermo Fisher Scientific (2 mentions) Mouse anti rabbit, by Jackson ImmunoResearch (2 mentions) Ab13970, by Abcam (1 mentions) Prolong diamond antifade mountant, by Thermo Fisher Scientific (1 mentions) Fv3000 confocal microscope, by Olympus (1 mentions) Mini protean tgx gel, by Bio-Rad (1 mentions) Odyssey software version 2, by LI COR (1 mentions) Gfp trap beads, by Proteintech (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Mouse α ha, by Merck Group (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Jackson ImmunoResearch (1 mentions) Mms 101p, by Abcam (1 mentions) Fluoview fv1000, by Olympus (1 mentions)

15 protocols using chicken α gfp

Immunofluorescence and Western Blot Protocols

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Primary antibodies were used at the following dilutions for immunofluorescence: chicken α-GFP (1:400; Abcam, Cambridge, MA), rabbit α-SYP-1 (1:200;(MacQueen et al., 2002 (link)), guinea pig α-HTP-3 (1:400; (Goodyer et al., 2008 (link)), rabbit α-AIR-2 (1:100;[de Carvalho et al., 2008 (link)]), rabbit α-LAB-1 (1:300;[de Carvalho et al., 2008 (link)]), mouse α-dpMPK-1 (1:500; Sigma, St. Louis, MO) and rabbit anti-RhoA (1:200; Santa Cruz). The following secondary antibodies from Jackson ImmunoResearch (Jackson ImmunoResearch, WestGrove, PA) were used at a 1:200 dilution: α-chicken FITC, α-rabbit Cy5, α-mouse FITC, and α-guinea pig FITC. Vectashield containing 1μg/μl of DAPI from Vector Laboratories was used as a mounting media and anti-fading agent.
Primary antibodies were used in the following dilutions for western blot analysis: chicken α-GFP (1:2000; Abcam), rabbit α-SYP-2 (1:200;[Colaiácovo et al., 2003 (link)]), rabbit α-SYP-3 (1:200; [Smolikov et al., 2007b (link)]), mouse α-dpMPK-1 (1:500; Sigma), mouse α-tubulin (1:2000; Sigma) and rabbit α-MPK-1 (1:2000; Santa Cruz, Dallas, TX). HRP-conjugated secondary antibodies, donkey anti-chicken, rabbit anti-mouse, and mouse anti-rabbit from Jackson ImmunoResearch were used at a 1:10,000 dilution.

Nadarajan S., Mohideen F., Tzur Y.B., Ferrandiz N., Crawley O., Montoya A., Faull P., Snijders A.P., Cutillas P.R., Jambhekar A., Blower M.D., Martinez-Perez E., Harper J.W, & Colaiacovo M.P. (2016). The MAP kinase pathway coordinates crossover designation with disassembly of synaptonemal complex proteins during meiosis. eLife, 5, e12039.

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Immunohistochemistry Staining Antibody Panel

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Primary antibodies were: Guinea pig α-Deadpan (1:1,000) and rat α-Dpn (1:200) [54 ]. Guinea pig α-Col (1:1,000), guinea pig α-Dimm (1:1,000), chicken α-proNplp1 (1:1000) [6 ]. Rat α-Nab (1:500) [20 (link)]. mAb α-Eya 10H6 (1:250) (Developmental Studies Hybridoma Bank, Iowa City, IA, US). Rabbit α-Ap (1:1,000) [35 (link)] (provided by D. Bieli and M. Affolter). Chicken α-GFP 1:1,000 (Abcam, ab13970).

Stratmann J, & Thor S. (2017). Neuronal cell fate specification by the molecular convergence of different spatio-temporal cues on a common initiator terminal selector gene. PLoS Genetics, 13(4), e1006729.

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Immunohistochemical Staining of Embryonic Tissue

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Embryos were fixed in 4% paraformaldehyde in PBS, cryoprotected in 30% sucrose in PBS and subsequently stored at -80°C. Sagittal sections (16 μm) were cut on a cryostat, after which they were washed with PBS and blocked in 4% Fetal Calf Serum (FCS) in THZT (50 mM Tris-HCl pH 7.6, 0.5 M NaCl, 0.5% Triton) or PBS-T (0.5% Triton). After another wash treatment with TBS, sections were incubated overnight at 4°C with primary antibody in THZT. Sections were washed three times (PBS) the following morning and incubated for minimally 2 hours at room temperature with secondary antibody in PBS, followed by wash treatment with PBS. DAPI staining was performed (1mg/ml 1:5000) for 5 min, after which section were washed with PBS. Finally, sections were embedded with Fluorsave.
Primary antibodies that were used: Rabbit-α-Th (Pelfreeze, 1:1000), Chicken-α-GFP (Abcam, 1:1000). Secondary antibodies that were used: Goat-α-Rabbit Alexa 555 (1:1000), Goat-α-Chicken Alexa 488 (1:1000), all Invitrogen.

Kouwenhoven W.M., von Oerthel L, & Smidt M.P. (2017). Pitx3 and En1 determine the size and molecular programming of the dopaminergic neuronal pool. PLoS ONE, 12(8), e0182421.

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Immunofluorescence Analysis of GFP in Lung Tissue

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Lung samples from untreated (negative control) and LV-treated mice were fixed in 4% paraformaldehyde, paraffin-embedded, sectioned at 5 µm, and de-paraffinised using standard histological procedures. Antigen retrieval was performed using 0.1 M EDTA (pH 8.0) for 10 min followed by permeabilisation in phosphate-buffered saline (PBS)/Triton X-100 (0.3%) for 10 min. Sections were blocked for 1 h at room temperature in a solution of 1% bovine serum albumin and 0.05% Tween-20. Primary antibody chicken α-GFP (1:100 dilution) (Abcam, ab13970) was resuspended in blocking buffer and incubated with samples overnight at 4 °C. No antibody and secondary antibody-only controls were included. Slides were washed followed by incubation with goat α-chicken Alexa Fluor® 568 (1:200) (Abcam, ab175711) in blocking buffer at room temperature for 1 h. Samples were washed followed by counterstaining with DAPI (1 µg/mL) and mounting with ProLong Diamond Antifade Mountant (Molecular Probes). Images were generated using an Olympus FV3000 confocal microscope.

Donnelley M., Cmielewski P., Knight E., Carpentieri C., McCarron A., Rout-Pitt N., Parsons D, & Farrow N. (2023). Repeat or single-dose lentiviral vector administration to mouse lungs? It’s all about the timing. Gene Therapy, 30(9), 698-705.

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GFP Immunoprecipitation of SPARC in Drosophila Ovaries

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Adult females were aged 3 days on yeast at 25°C and dissected in S2 media. Ovaries from 25 females per genotype were collected and lysed in cold modified RIPA buffer (50mM Tris pH 7.8, 100 mM NaCl, 2 mM CaCl₂, 0.1% SDS, 0.5% Sodium Deoxycholate, 1% triton) + complete protease inhibitor cocktail (Roche) by manual grinding and passage through a 27-gauge needle. Lysate was centrifuged at 13000 RPM and supernatant collected. GFP immunoprecipitation reactions were performed using GFP-Trap beads (Chromotek) at 4°C overnight. Input lysate and immunoprecipitate were analyzed via Western Blot on a 4–15% Mini-PROTEAN TGX Gel (Bio-Rad) using the following antibodies: rabbit α-SPARC (1:1500) (Martinek et al., 2002 (link)), chicken α-GFP (1:10,000, abcam). IRDye (LI-COR) secondary antibodies were used at 1:5000. Blots were imaged with Odyssey software version 2.1 (LI-COR Biosciences).

Isabella A.J, & Horne-Badovinac S. (2015). Dynamic regulation of basement membrane protein levels promotes egg chamber elongation in Drosophila. Developmental biology, 406(2), 212-221.

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Acetylated Histone Detection Protocol

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Whole worm lysates were prepared from young adult worms (24 hours post-L4) by freezing and then boiling the worms in Laemmli sample buffer. Proteins were resolved by SDS-PAGE and then transferred onto polyvinylidene difluoride membranes (Millipore, 0.2 μm pore size) in transfer buffer (25 mM Tris-HCl pH 8.3, 192 mM glycine, 20% (v/v) methanol and 0.1% (w/v) SDS). The presence of SDS ensures histones can be completely transferred onto the membrane. Antibodies were used at the following dilutions: chicken α-GFP (Abcam, 1:2000), mouse α-HA (Sigma, 1:2000), rabbit α-AcK (1:3000), rabbit α-H3ac (Active motif, 1:3000), rabbit α-H4ac (Active motif, 1:3000), rabbit α-H3 (Cell signaling, 1:5000), rabbit α-H3K56ac (Millipore, 1:3000), mouse α-tubulin (Sigma, 1:2000), rabbit α-ACER-1(1:3000). Horseradish peroxidase-conjugated secondary antibodies from Jackson ImmunoResearch Laboratories were used at a 1:5000 dilution. Specific proteins were visualized with Pierce ECL Western Blotting Substrate. The relative level of acetylated histones was determined by densitometric analysis of the western blot bands (AcK relative to H3) using ImageJ software.

Gao J., Kim H.M., Elia A.E., Elledge S.J, & Colaiácovo M.P. (2015). NatB Domain-Containing CRA-1 Antagonizes Hydrolase ACER-1 Linking Acetyl-CoA Metabolism to the Initiation of Recombination during C. elegans Meiosis. PLoS Genetics, 11(3), e1005029.

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Generating Drosophila Neuroblast MARCM Clones

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To generate Drosophila neuroblast MARCM clones, FRT-G13, aPKC^K06403/CyO Virgin flies were crossed to ;;3xHA-aPKC V606A male flies. The resulting non-Cyo male progeny were crossed to elav-Gal4, UAS-mCD8:GFP, hs:flp; FRT-G13, tubPGal80 Virgins and allowed to lay for 24 hours at room temperature. The vials were then allowed to stay at room temperature for an additional 24 hours at which time they were heat-shocked @37°C for 90 minutes. This was followed by a possible second 90 minute heat-shock within 18 hours. Vials were raised at 18°C or room temperature until wandering third instar stage when they were dissected and stained as described above with the following antibodies: Primary antibodies: Rat α-Mira (1:500; Abcam, ab197788), Rabbit α-HA C29F4(1:1,000; Cell Signaling Technologies, 3724) or Mouse α-HA (1:500; Covance, MMS-101P), and Chicken α-GFP (1:500; Abcam, ab13970). Secondary antibodies: Dk α-Rt Cy3 (712-165-153; 1:500), Dk α-Rb 647 (711-605-152; 1:500) or Dk α-Ms 647 (715-605-151; 1:500), and Dk α-Ck 488 (703-545-155). Brains were imaged using a Leica TCS SPE upright confocal microscope using an ACS APO 40× 1.15 NA Oil CS objective or an Olympus Fluoview FV1000 upright confocal microscope using a PlanApo N 60× 1.42 NA Oil objective.

Holly R.W., Jones K, & Prehoda K.E. (2020). A conserved PDZ Binding Motif in aPKC interacts with Par-3 and mediates cortical polarity. Current biology : CB, 30(5), 893-898.e5.

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Immunofluorescence Staining of Frozen Tissue

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Frozen tissue blocks were sectioned at 14 μm and mounted on Fisher permafrost slides. Immunohistochemistry using fluorescent labeled antibodies was performed as described [13 (link)]. Primary antibodies used were: mouse α-Nkx2.2 (DSHB 1:100), α -Foxa2 (DSHB, 1:100), and α-Myc (DSHB 1:200); rabbit α -Olig2 (1:6000; a gift from H. Takebayashi, Kyoto University, Kyoto, Japan), and α -Nkx2.2 (a gift from Tom Jessell, 1:4000); chicken α-GFP (Abcam 1:1000).

Wang H, & Matise M.P. (2016). Tcf7l2/Tcf4 Transcriptional Repressor Function Requires HDAC Activity in the Developing Vertebrate CNS. PLoS ONE, 11(9), e0163267.

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Zebrafish Immunohistochemistry for Labeling Proteins

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Zebrafish embryos and larvae were fixed in 4% PFA/1x PBS at 4° C overnight, and then incubated with 150 mM Tris-HCl, pH 9.0 at 70° C for 15 minutes for antigen retrieval^{52 (link)}. Samples were then permeabilized with 100% acetone at −20° C for 20 minutes, and antibody staining was performed via standard procedures^{50 (link)}. The following primary antibodies used: chicken α-GFP (Abcam, 1:1000), rabbit α-RFP (Rockland, 1:1000), mouse α-SV2 (DSHB, 1:200), and mouse α-GS (Sigma, 1:1 prediluted). The following secondary antibodies used: Alexa 488 α-chicken (Jackson ImmunoResearch, 1:250), Rhodamine Red-X α-rabbit (Jackson ImmunoResearch, 1:250), and Dylight 649 α-mouse (Vector Laboratories, 1:250). Stained samples were mounted in Vectashield antifade mounting medium (Vector Laboratories) for confocal analysis.

Chen J., Poskanzer K.E., Freeman M.R, & Monk K.R. (2020). Live-imaging of astrocyte morphogenesis and function in zebrafish neural circuits. Nature neuroscience, 23(10), 1297-1306.

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Zebrafish Immunohistochemistry for Labeling Proteins

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Chen J., Poskanzer K.E., Freeman M.R, & Monk K.R. (2020). Live-imaging of astrocyte morphogenesis and function in zebrafish neural circuits. Nature neuroscience, 23(10), 1297-1306.

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