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Anti gfp

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Anti-GFP is a laboratory product used for the detection and enrichment of Green Fluorescent Protein (GFP) in biological samples. It functions as an antibody that specifically binds to GFP, enabling the identification and isolation of GFP-tagged proteins or cells.

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Lab products found in correlation

Anti tubulin, by Merck Group (3 mentions) Anti p erk, by Cell Signaling Technology (2 mentions) Flag ubiquitin, by R&D Systems (1 mentions) Anti ha, by Merck Group (1 mentions) Anti synaptophysin, by Synaptic Systems (1 mentions) Anti psd95, by Cell Signaling Technology (1 mentions) Anti actin, by Abcam (1 mentions) Anti n cadherin, by Cell Signaling Technology (1 mentions) Anti rab11, by Cell Signaling Technology (1 mentions) Anti ho 1, by Cell Signaling Technology (1 mentions) Anti sorcs2, by R&D Systems (1 mentions) Anti eaat3, by Cell Signaling Technology (1 mentions) Mab2263, by Merck Group (1 mentions) Alexa fluor 568 goat anti mouse igg, by Thermo Fisher Scientific (1 mentions) Anti gfp, by Nacalai Tesque (1 mentions) Alexa fluor 488 goat anti rat, by Thermo Fisher Scientific (1 mentions) Anti ncl antibody, by Abcam (1 mentions) Anti npm antibody, by Thermo Fisher Scientific (1 mentions) Pm036, by MBL Life Science (1 mentions) Anti lc3, by MBL Life Science (1 mentions)

7 protocols using anti gfp

1

Immunostaining of Fluorescent Markers in Larvae

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The following antibodies were used for immunostaining: anti-GFP (1:1000, rat, Nacalai Tesque, Japan, Cat# 04404-84) or anti-GFP (1:1000, rabbit, MBL international, Cat# 598) for BoTxBLC-GFP, anti-GFP (1:1000, rabbit, MBL international) for GCaMP7a, anti-Neurod1 (1:400, mouse, ascites)17 (link), and anti-parvalbumin 7 (1:1000, mouse monoclonal, ascites)14 (link). Larvae and cryostat sections were immunostained as described previously14 (link), 17 (link). The following secondary antibodies were used: Alexa Fluor 488 goat anti-rat (H + L, Molecular Probes, Thermo Fisher Scientific, USA, Cat#A11006), CF488A anti-rabbit (H + L, Biotium Inc., USA, Cat#20019), and Alexa Fluor 568 goat anti-mouse IgG (H + L, Molecular Probes, Thermo Fisher Scientific, USA, Cat#A11031). Some fixed samples were optically cleared with SeeDB reagent as previously reported45 (link), 46 .
Matsuda K., Yoshida M., Kawakami K., Hibi M, & Shimizu T. (2017). Granule cells control recovery from classical conditioned fear responses in the zebrafish cerebellum. Scientific Reports, 7, 11865.
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2

FBXO21-Mediated p85α Ubiquitylation

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HEK293T cells were transfected with plasmids encoding HA-FBXO21, HA-ΔFBXO21, or GFP-p85α. 48 h post transfection, HA-FBXO21, HA-ΔFBXO21, or GFP-p85α were immunopurified from the whole cell extracts using Anti-HA (Sigma) or Anti-GFP (MBL International) beads overnight at 4 °C. The immunopurified HA-FBXO21 or HA-ΔFBXO21 (0.5 µg) proteins were incubated with immunopurified GFP-p85α (0.5 µg), E1 (500 ng), E2-UbcH5a (500 ng), FLAG-ubiquitin (0.5 µg) (BostonBiochem), and ATP (10 mM). Ubiquitylation reactions were performed in 100 mM NaCl, 1 mM DTT, 5 mM MgCl2, 25 mM Tris-Cl (pH 7.5), incubated at 30 °C for 2 h, and stopped with 2× laemmli buffer (10 min at 95 °C).
Dobish K.K., Wittorf K.J., Swenson S.A., Bean D.C., Gavile C.M., Woods N.T., Ghosal G., Hyde R.K, & Buckley S.M. (2023). FBXO21 mediated degradation of p85α regulates proliferation and survival of acute myeloid leukemia. Leukemia, 37(11), 2197-2208.
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3

Comprehensive Western Blot Analysis

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Tissue and cell lysates were analyzed by western blot using the following antibodies: anti-SorCS2 (R&D Systems, AF4237, 1:1000), anti-EAAT3 (Cell Signaling, #14501, 1:1000), anti-p-ERK (Cell Signaling, #4370, 1:2000), anti-tubulin (EMD Millipore, CP06, 1:5000), anti-mGlur2/3 (Novus Biologicals, NB300-124, 1:1000), anti-actin (Abcam, ab8227, 1:2000), anti-JWA (Trans Genic, KR057, 1:250), anti-N-cadherin (Cell Signaling, #14215, 1:1000), anti-GFP (MBL International, MBL598, 1:2000), anti-Rab11 (Cell Signaling, #5589, 1:1000), anti-synaptophysin (Synaptic Systems, 101011, 1:5000), anti-GluA1 (EMD Millipore, MAB2263, 1:1000), anti-GluA2 (EMD Millipore, MABN71, 1:1000), anti-PSD95 (Cell Signaling, #3409, 1:1000), anti-HO-1 (Cell Signaling, #70081, 1:1000). After incubation with secondary antibodies coupled to HRP, chemiluminescent signal was registered with use of digital LI-COR imaging system.
Malik A.R., Szydlowska K., Nizinska K., Asaro A., van Vliet E.A., Popp O., Dittmar G., Fritsche-Guenther R., Kirwan J.A., Nykjaer A., Lukasiuk K., Aronica E, & Willnow T.E. (2019). SorCS2 Controls Functional Expression of Amino Acid Transporter EAAT3 and Protects Neurons from Oxidative Stress and Epilepsy-Induced Pathology. Cell Reports, 26(10), 2792-2804.e6.
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4

Antibody Validation for Autophagy Proteins

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The anti-GFP, anti-p62/SQSTM1, anti-BECN1, anti-ATG5 and anti-LC3 antibodies were purchased from MBL International (Woburn, MA, USA) (598, PM045, PM017, M153-3 and PM036, respectively). Anti-β-actin and anti-p53 antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA) (sc-47778 and sc-126, respectively). The anti-NCL antibody was purchased from Abcam (Cambridge, MA, USA) (ab-13541) and anti-NPM antibody was purchased from Invitrogen (32-5200).
Katagiri N., Kuroda T., Kishimoto H., Hayashi Y., Kumazawa T, & Kimura K. (2015). The nucleolar protein nucleophosmin is essential for autophagy induced by inhibiting Pol I transcription. Scientific Reports, 5, 8903.
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5

Immunoblotting Protocol for Centromeric Proteins

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Cells were suspended in lysis buffer (50 mM Na Phosphate pH 8.0, 30 mM NaCl, 0.1% NP40, 5 mM β-mercaptoethanol, protease inhibitors (Roche) and phosphatase inhibitors) and then resuspended in 2 × SDS loading buffer. The following antibodies were used for immunoblotting: anti-GFP (1:2,500, MBL international), anti-Hec1(1:1,500, Abcam), anti-tubulin (1:4,000, Sigma), anti-CENP-T (1:5,000), anti-CENP-C (1:5,000), horseradish peroxidase-conjugated anti-rabbit IgG (1:100,000, Jackson ImmunoResearch) and horseradish peroxidase-conjugated anti-mouse IgG (1:100,000, Jackson ImmunoResearch)13 (link)35 (link).
Suzuki A., Badger B.L, & Salmon E.D. (2015). A quantitative description of Ndc80 complex linkage to human kinetochores. Nature Communications, 6, 8161.
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6

PD-1-PD-L1 Signaling Pathway Analysis

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DC-1 cells were prepulsed with 5 μM MCC88-103 overnight at 37 °C and washed before the assay. 2 × 106 mPD-1-deleted 2D12 cells transduced with hPD-1 were stimulated with 2 × 106 DC-1 cells not transduced or transduced with hPD-L1. The cells were lysed with the lysis buffer (50 mM Tris-HCl, 50 mM NaCl, and 5 mM EDTA) containing 1% NP-40. Whole cell lysates (WCLs) or those immunoprecipitated by anti-GFP (MBL International, D153-11, RRID:AB_2893312) were blotted with anti-GFP (1:5000, Miltenyi Biotec, 130-091-833, RRID:AB_247003), anti-mSHP1 (1:500, Santa Cruz Biotechnology, sc-287, RRID:AB_2173829), anti-mSHP2 (1:1000, Santa Cruz Biotechnology Inc., sc-7384, RRID:AB_628252), anti-PLCγ (1:1000, Cell Signaling Technology, 5690, RRID:AB_10691383), anti-pPLCγ (1:1000, Cell Signaling Technology, 8713, RRID:AB_10890863), anti-Akt (1:2000, Cell Signaling Technology, 4691, RRID:AB_915783), anti-pAkt (1:1000, Cell Signaling Technology, 4060, RRID:AB_2315049), anti-Erk (1:1000, Cell Signaling Technology, 4695, RRID:AB_390779), or anti-pErk (1:1000, Cell Signaling Technology, 4370, RRID:AB_2315112) as a first antibody and HRP-anti-rabbit IgG polyclonal Abs (1:10,000, Cell Signaling Technology, 7074, RRID:AB_2099233) as a second one. Each intensity of band was calculated by ImageJ (RRID:SCR_003070).
Nishi W., Wakamatsu E., Machiyama H., Matsushima R., Saito K., Yoshida Y., Nishikawa T., Takehara T., Toyota H., Furuhata M., Nishijima H., Takeuchi A., Azuma M., Suzuki M, & Yokosuka T. (2023). Evaluation of therapeutic PD-1 antibodies by an advanced single-molecule imaging system detecting human PD-1 microclusters. Nature Communications, 14, 3157.
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7

Cilia Localization Assays for Protein Regulators

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For Gpr161, Smo or Gli2 cilia localization assays, IMCD3, NIH-3T3, Smo-GFP, Smo-M2-myc, or SmoL412F-myc cells were grown to confluence on 12mm poly-L-Lysine pre-coated glass coverslips (BD Biosciences). The indicated compounds were dissolved in DMEM/3%CS and then applied to cells for 48hrs or 72hrs. Cells were either fixed in 100% methanol for 5min at −20°C or in 3.7% formaldehyde for 15min at room temperature. The cells were further permeabilized in blocking buffer (5% normal goat serum and 0.2% Triton X-100 in PBS) for 10min. Coverslips were treated with anti-Smo (provided by P. A. Beachy), anti-Myc (Cell Signaling Technology, 2272), anti-GFP (MBL International, 598), anti-Gli2 and anti-Gpr161 (provided by S. Scales, Genentech), and anti-tubulin (Sigma, T6793) in blocking buffer each for 30min. After several PBS washes, the coverslips were further incubated with Alexa Fluor 488-conjugated goat anti-rabbit, Alexa 594-conjugated goat anti-mouse, or Hoechst 33342 (Invitrogen) for 30min. 100 primary cilia were scored for the presence of Gpr161, Smo, SmoM2, SmoL412F, and Gli2 in each experiment.
Fan C.W., Chen B., Franco I., Lu J., Shi H., Wei S., Wang C., Wu X., Tang W., Roth M.G., Williams N.S., Hirsch E., Chen C, & Lum L. (2014). The Hedgehog pathway effector Smoothened exhibits signaling competency in the absence of ciliary accumulation. Chemistry & biology, 21(12), 1680-1689.
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