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1 299 protocols using flag tag (flag)

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Chromatin Immunoprecipitation (ChIP) Protocol

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Example 6

Cells dimerized as described above were collected and spun down prior to crosslinking with 1% formaldehyde at room temperature for 10 minutes followed by glycine quenching. Cells were lysed in 0.1 M Tris pH 7.5, 10 mM potassium acetate, 15 mM magnesium acetate, 1% NP-40 and spun to isolate nuclei, then nuclei were lysed using 0.1 M Tris pH 8, 1% SDS, 10 mM EDTA. Nuclei were sonicated briefly to solubilize material, and SDS was quenched with dilution buffer containing 0.01% SDS, 1.1% Triton X-100, 1.2 mM EDTA, 16.7 mM Tris pH 7.5, and 167 mM NaCl. Protein complexes were immunoprecipitated overnight using the antibodies against HA (Cell Signaling 3724), Flag (Sigma F1804), or DDX5 (Bethyl A300-523A), all at 1:50, and were washed three times with 100 mM Tris pH 9, 100 mM LiCl, 1% NP-40, and 1% sodium deoxycholate. Complexes were eluted by vortexing twice with 1% SDS, 15 mM NaHCO3 for 15 minutes each time. Elutes were run on SDS-page gels and probed with antibodies against the HA tag (Cell Signaling 3724), Flag tag (Sigma F1804), CTCF (Cell Signaling 2899), SMC1 (Bethyl A300-055A), or DDX17 (Bethyl A300-509A) as indicated, all at 1:1000.

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Multiparametric Immunostaining and Western Blotting

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The primary antibodies used in immunostaining were as follows: RNF20 (21615-1-AP; Proteintech, Rosemont, IL, USA), NESTIN (MAB353; Millipore, Darmstadt, Germany), ACSBG1 (ab118154; Abcam, Cambridge, UK), GFAP (G6171; Sigma, St. Louis, MO, USA), GFAP (Z0334 Dako, Santa Clara, CA, USA), GFAP (60190-1-Ig; Proteintech), GLAST (BMP009; MBL, Beijing, China), Tenascin C (110-68136; NB, Littleton, CO, USA), Ki67 (ab137876; Abcam), FLAG (F1804; Sigma), STAT3 (#9139; Cell Signaling Technology, Beverly, MA, USA). The primary antibodies used in western blotting were as follows: RNF20 (21615-1-AP; Proteintech), GLAST (20785-1-AP; Proteintech), ACSBG1 (ab118154; Abcam), GFAP (G6171; Sigma), STAT3 (#9139; Cell Signaling Technology), phospho-STAT3 (#9145; Cell Signaling Technology), Ubiquityl-Histone H2B (Lys 120) (#5546; Cell Signaling Technology), H4K16ac (07-329; Millipore), H3K9me3 (07-442; Millipore), Trimethyl-Histone H3 (Lys 27) (07-449; Millipore), H2B (ab1790; Abcam), FLAG (F1804; Sigma), HA (M20003; Abmart, Shanghai, China), β-ACTIN (20536-1-AP; Proteintech). Alexa-conjugated secondary antibodies (Jackson ImmunoResearch, West Grove, PA, USA) were used for immunostaining. IR Dye (LI-COR Biosciences, Lincoln, Nebraska, USA) 800 CW donkey anti-rabbit and 680 CW donkey anti-mouse secondary antibodies were used in western blotting.
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3

Immunoprecipitation of Myo1D and Dronc

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Figure 3E: Because the available Myo1D
antibody did not perform in IP experiments, UAS-Myo1D-GFP was crossed
into ey>hid,p35 background and IP experiments were performed with
GFP-Trap_M beads (15μl, Chromotek) from larval extracts. Immunoprecipitates were
separated on 4–15% gradient SDS-PAGE and blotted on PVDF membranes. GFP
(1:1000; Pierce) and Dronc (SK11) (1:1000; gift of P. Meier) antibodies were used for
immunoblotting. For the reverse experiment (Figure
3F
), Flag-Dronc and Myo1D-HA were crossed
into ey-Gal4 background and immunoprecipitates using anti-Flag M2
magnetic beads (35μl, Sigma-Aldrich) were separated by SDS-PAGE. Immunoblots
were probed with HA (1:1000; Pierce) and Flag (1:1000, Sigma-Aldrich) antibodies. For
Figure 3H, total extracts of
ey>hid,p35,Myo1D-GFP and
ey>hid,p35,Myo1D-GFP,Flag-Dronc imaginal discs were analyzed by
immunoblotting with GFP antibodies.
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4

Immunofluorescence Staining Protocol for Bacteria

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Coverslips with fixed cells were blocked and permeabilized in 5% nonfat milk in PBS + 0.1% saponin for 30 min. Coverslips were then stained with primary antibody diluted in PBS with 5% milk and 0.1% saponin for 2 to 4 h. Primary antibodies used in this study were FLAG (Clone M2, Sigma-Aldrich, F1804; 1:1000), FLAG (Sigma-Aldrich, F7425; 1:1,000), HA (Roche, 11867423001; 1:1000), LC3 (Invitrogen, L10382; 1:250), ubiquitin (clone FK2; Millipore Sigma, 04-263; 1:500), p62 (Bethyl, A302-855A; 1:500), p62 (Abcam, ab56416, 1:500), TAX1BP1 (Bethyl, A303-791A; 1:500), OPTN (Bethyl, A301-829A; 1:500), and GFP (Abcam, ab183734; 1:500). Coverslips were washed three times in PBS and stained with secondary antibodies (goat anti-rabbit Alexa Fluor 488, goat anti-rat Alexa Fluor 647, and/or goat anti-mouse Alexa Fluor 647; Invitrogen, 1:1,000) and DAPI (1:10,000) in PBS–5% milk–0.1% saponin for 1 to 2 h. Coverslips were then washed twice with PBS and twice with water and mounted using Prolong Gold Antifade Mountant (Thermo Fisher). Cells were imaged on an Olympus Fluoview FV3000 confocal laser scanning microscope. Three coverslips per genotype were imaged, and at least 300 bacteria per coverslip were assessed and counted.
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5

Comprehensive Immunoblotting and Immunoprecipitation Procedures

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The following primary Abs were used for immunoblotting: NLRP3 (Cell Signaling 13158, 1:1000), IL-1β (Cell Signaling 12703, 1:1000), GFP (Cell Signaling 2955, 1:1000), TFEB (Cell Signaling 4240, 1:1000), CHOP (Cell Signaling 2895, 1:1000), LC3A/B (Cell Signaling clone D3U4C, 1:1000) Histone H3 (Cell Signaling clone D1H2, 1:2000), Myc (EMD Millipore clone 9E10, 1:2000), Flag (Sigma F1804, 1:1000), ASC (Santa Cruz sc-22514, 1:1000), LAMP1 (Santa Cruz clone H3A4, 1:2000), GAPDH-HRP (ProteinTech HRP-60004, 1:5000), and actin-HRP (Sigma A3854, 1:10,000). Anti-mouse (Cell Signaling 7076) or anti-rabbit (Cell Signaling 7074) HRP-conjugated secondary antibodies were used for ECL based detection. Primary Abs for immunofluorescence were NLRP3 (Enzo AlX-804-819), ASC (Santa Cruz sc-22514), ERp72 (Cell Signaling D70D12), and TGN38 (Novus, NBP1-03495). Alexa 568 conjugated polyclonal anti-mouse (Thermo Fisher, A11004) and anti-rabbit (Thermo Fisher, A11011) were used as secondary Abs prior to fluorescent imaging. For immunoprecipitation experiments, we used GFP antibodies coupled to magnetic beads (MBL, D153-9) and Flag antibodies coupled to agarose (Sigma, A2220) to pull down tagged proteins prior to immunoblotting. Cyclosporin A (R&D Systems, 1101) and Z-VAD-FMK (Sigma, V116) were used at 10 μM overnight, and Bafilomycin A1 (Sigma, B1793) at 100 nM for 4 h.
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6

Comprehensive Antibody Panel for Cellular Signaling Analysis

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Primary antibodies included antibodies to S6K1 (Abcam 32359), pS6K-Thr389 (CST 9205), p4EBP1-Ser65 (CST 9451), 4EBP1 (CST 9644), pan AKT (CST 4691), pAKT-Thr308 (CST 2965), AKT1 (CST 2938), pAKT substrate (RXRXXpS*/T*) (CST 10001), GAPDH (CST 5174), flag (Sigma F1804), flag (Sigma A9594), HA (CST 3724), HA (CST 3444), GST (CST 2625), Ub (Santa Cruz sc-8017), c-Myc (Santa Cruz sc-40), RNF167 (Santa Cruz sc-515405), RNF167 (Proteintech 24618-1-AP), and β-tubulin (Sigma 7B9). Antibodies to CASTOR1 were described as before13 . Secondary antibodies included mouse anti-Rabbit IgG (Light-Chain Specific) (CST 93702), rabbit anti-Mouse IgG (Light Chain Specific) (CST 58802), goat anti-rabbit horseradish peroxidase (HRP)-conjugated IgG (CST 7074), horse anti-mouse IgG HRP-conjugated IgG (CST 7076), goat anti-mouse IgG DyLight 800 (Bio-Rad STAR117D800GA), and goat anti-rabbit IgG StarBright Blue700 (Bio-Rad 12004161).
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7

PALB2 Interactome Characterization in 293T Cells

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The pOZ-FH-C1-PALB2 constructs were transfected into 293 T cells using the Liposomal transfection reagent (Yeasen, Shanghai, China). After 48 h of transfection, cells were lysed with IP Lysis Buffer (Thermo Fisher Scientific, Waltham, MA, USA) supplemented with protease inhibitors (Thermo Fisher Scientific, Waltham, MA, USA). The FLAG-tagged PALB2 were IPed with anti-FLAG M2 magnetic beads (Sigma, St. Louis, MO, USA) overnight. For western blotting analyses, protein lysates were separated by 8–10% SDS-PAGE, transferred to PVDF membranes and probed with relevant antibodies, followed by ECL detection. The antibodies used were FLAG (Sigma Cat# F1804, 1:1000, St. Louis, MO, USA), PALB2 (Absin Cat# abs120051, 1:500, Shanghai, China), BRCA1 (Millipore Cat# 07-434, 1:5000, Burlington, MA, USA), RAD51 (Abcam Cat# ab133534, 1:5000, Cambridge, UK), and GAPDH (Boster Cat# BM1985, 1:2000, Pleasanton, CA, USA). Relative protein expression was determined using ImageJ.
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8

Antibody Production and Characterization

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Rabbit polyclonal antibodies to C-terminal 19-aa residues of Pex14p (Shimizu et al., 1999 (link)), Pex13p (Mukai and Fujiki, 2006 (link)), Pex3p (Ghaedi et al., 2000 (link)), acyl-CoA oxidase (Tsukamoto et al., 1990 (link)), HA (Otera et al., 2000 (link)), LC3 (MBL), cathepsin D (a gift from K. Kato; Nishimura et al., 1987 (link)), and guinea pig anti-Pex14p antibody (Mukai et al., 2002 (link)) were used. Rabbit antiserum to the insertion 1 in human Miro1-var2 and Miro1-4, termed anti–Miro1-ins1 antibody, was raised by conventional subcutaneous injection of a synthetic 32-aa peptide (EDHYRDRLSRDMGHTDRIENLRKIWVFLKTAF) that had been linked to keyhole limpet hemocyanin (Tsukamoto et al., 1990 (link)). Rabbit antibody was purified by affinity chromatography using a CL-4B column (GE Healthcare) conjugated to GST-Miro1–insertion 1 encompassing the 32-aa sequence according to the manufacturer’s instructions. The following primary antibodies were purchased: rabbit polyclonal antibodies to FLAG (Sigma-Aldrich) and Miro1/2 (Santa Cruz Biotechnology, Inc.), mouse monoclonal antibodies to HA (16B12; Covance), FLAG (Sigma-Aldrich), cytochrome P450 reductase (F-10; Santa Cruz Biotechnology, Inc.), α-tubulin (Abcam), and Tom20 (Santa Cruz Biotechnology, Inc.), and goat anti–lactate dehydrogenase antibody (Rockland).
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Antibody Profiling for Protein Analysis

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The following monoclonal antibodies were used in this study: FMRP 1C3 (WB, 1:1000, Millipore, Hayward, CA, USA), FMRP 7G1-1 (WB, 1:500, DSHB), and Flag (IP, Sigma, Saint Louis, MO, USA). The following rabbit polyclonal antibodies were used in this study: Flag (WB, 1:1000, Sigma, Saint Louis, MO, USA), GFP (WB, 1:5000, Abcam, Cambridge, MA, USA), and FMRP (WB, IP, 1:1000, Abcam, Cambridge, MA, USA). A chicken polyclonal antibody for GFP (WB, 1:5000, Abcam, Cambridge, MA, USA) was also used. The antibody for T7 was directly conjugated to HRP (WB, 1:5000, Millipore, Hayward, CA, USA). Anti-mouse IgG-HRP, anti-rabbit IgG-HRP, and protein-HRP (1:5000, Jackson Labs, West Grove, PA, USA) were used for ECL detected Western blots. For Licor imaging, IRDye anti-mouse IgG-800CW and IRDye anti-rabbit IgG-680RD was used (1:10,000, Licor, Lincoln, NE, USA).
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Co-immunoprecipitation and ChIP Protocols

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Co-immunoprecipitation was carried out with antibodies to FLAG (M2, Sigma), V5 (Invitrogen), Lin28A (Abcam) or Tet1 (Millipore) as described (Kim et al., 2009 (link)). Five million mESCs were used for Chip following procedures as described (Ma et al., 2009 (link)) with antibodies to FLAG (M2, Sigma), HA (Sigma), Lin28A (Abcam) or Tet1 (Millipore), or normal mouse or Rabbit IgG (Millipore) as a control.
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