GFP-Trap® A

Details for Product No. ABIN509397
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Target Name (Antigen)
Reactivity
Aequorea victoria
(21)
Host
Camelidae
Conjugate
Agarose Beads
Application
Protein Complex Immunoprecipitation (Co-IP), Mass Spectrometry (MS), Enzyme Activity Assay (EAA), Affinity Measurement (AM), Chromatin Immunoprecipitation (ChIP), Pull-Down Assay (Pull-Down), Purification (Purif), Immunoprecipitation (IP)
Pubmed 99 references available
Quantity 20 tests
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Catalog No. ABIN509397
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Purpose GFP-Trap® is a high quality GFP-binding protein coupled to a monovalent matrix (agarose beads) for biochemical analysis of GFP fusion proteins and their interacting partners.
Brand GFP-Trap®
Sample Type Cell Extracts
Fragment heavy chain antibody (hcAb)
Specificity Binding capacity: 10 µL GFP-Trap®_A slurry binds 2.5 – 3 µg of GFP
Cross-Reactivity (Details) GFP-Trap® specifically binds to eGFP, wtGFP, GFP S65T, TagGFP, eYFP, YFP, Venus, Citrin, CFP. No binding to proteins derived from DsRed, all RFPs and TurboGFP can be detected.
Characteristics Antibodies – extremely powerful tools in biomedical research – are large complex molecules (~ 150 kDa) consisting of two heavy and two light chains. Due to their complex structure, the use of antibodies is often limited and hindered by batch-to-batch variations.

Camelidae (camels, dromedaries, llamas and alpacas) possess functional antibodies devoid of light chains, so-called heavy chain antibodies (hcAbs). hcAbs recognize and bind their antigens via a single variable domain (VHH). These VHH domains are the smallest intact antigen binding fragments (~ 13 kDa).

Nano-Traps are based on single domain antibody fragments (VHHs) derived from alpaca.
Components GFP-Trap® coupled to agarose beads
Material not included Lysis buffer (CoIP), 10x RIPA buffer, Dilution buffer, Wash buffer, Elution buffer
Alternative Name GFP
Background The green fluorescent protein (GFP) and variants thereof are widely used to study the subcellular localization and dynamics of proteins. GFP fusion proteins can be expressed in different cell types at different expression levels by transient or stable transfection. Transient expression may provide quick informative results, however, in many cases it is necessary to generate stable cell lines that express the GFP fusion protein of interest at a level similar to the one of the endogenous protein. Quantification of GFP fusion proteins in cells can be tricky since existing methods, like fluorescence microscopy or Western Blotting, are often shows insufficient signal to noise ratios or high signal variabilities .
Research Area Tags/Labels
Application Notes Green fluorescent proteins (GFP) and variants thereof are widely used to study protein localization and dynamics. For biochemical analyses including mass spectroscopy and enzyme activity measurements these GFP-fusion proteins and their interacting factors can be isolated fast and efficiently (one step) via Immunoprecipitation using the GFP-Trap®. The GFP-Trap®_A enables purification of any protein of interest fused to GFP.

Antibodies – extremely powerful tools in biomedical research – are large complex molecules (~ 150 kDa) consisting of two heavy and two light chains. Due to their complex structure, the use of antibodies is often limited and hindered by batch-to-batch variations.
Camelidae (camels, dromedaries, llamas and alpacas) possess functional antibodies devoid of light chains, so-called heavy chain antibodies (hcAbs). hcAbs recognize and bind their antigens via a single variable domain (VHH). These VHH domains are the smallest intact antigen binding fragments (~ 13 kDa).
Comment

Bead size ~ 90 µm

Protocol
  • Robust and versatile tool for biochemical analyses of GFP-fusion proteins
  • Short incubation times (5 – 30 min)
  • Quantitative isolation of fusion proteins and transiently bound factors from cell extracts or organelles
  • Low unspecific binding
  • No contaminating heavy and light chains of conventional antibodies
  • Applicable in Chromatin Immunoprecipitation (ChIP)
Reagent Preparation Suggested buffer composition

  • Lysis buffer (CoIP): 10 mM Tris/Cl pH 7.5, 150 mM NaCl, 0.5 mM EDTA,0.5% NP-40
  • 10x RIPA buffer: 10 mM Tris/Cl pH 7.5, 150 mM NaCl, 5 mM EDTA, 0.1% SDS, 1% Triton X-100, 1% Deoxycholate
  • Dilution buffer: 10 mM Tris/Cl pH 7.5, 150 mM NaCl, 0.5 mM EDTA
  • Wash buffer: 10 mM Tris/Cl pH 7.5, 150 mM NaCl, 0.5 mM EDTA
  • Elution buffer: 200 mM glycine pH 2.5
Assay Procedure Before you start: Add 1ml PBS to your cells and scrape them off the petri dish.Transfer to precooled tube, spin 3 min at 500 x g and discard supernatant. Wash cell pellet twice with ice cold PBS, briefly resuspending the cells.
  • 1. For one immunoprecipitation reaction resuspend cell pellet (~10^7 mammalian cells) in 200 µL lysis buffer by pipetting (or using a syringe).
    optional: add 1 mM PMSF and Protease inhibitor cocktail (not included) to lysis buffer
    optional for nuclear/chromatin proteins: add 1 mg/ml DNase and 2.5 mM MgCl2 (not included) to lysis buffer
  • 2. Place the tube on ice for 30 min with extensively pipetting every 10 min.
  • 3. Spin cell lysate at 20.000x g for 5 -10 minutes at 4°C.
  • 4. Transfer supernatant to a pre-cooled tube. Adjust volume with dilution buffer to 500 µL – 1000 µL. Discard pellet.
    optional: add 1 mM PMSF and Protease inhibitor cocktail (not included) to dilution buffer
    note: the cell lysate can be frozen at this point for long-term storage at -80°C For immunoblot analysis dilute 50 µL cell lysate with 50 µL 2x SDS-sample buffer(à refer to as input).
  • 5. Equilibrate GFP-Trap®_A beads in dilution buffer. Resuspend 20 - 30 µL bead slurry in 500 µL ice cold dilution buffer and spin down at 2.500x g for 2 minutes at 4°C. Discard supernatant and wash beads 2 more times with 500 µL ice cold dilution buffer.
  • 6. Add cell lysate to equilibrated GFP-Trap®_A beads and incubate the GFP-Trap®_A beads with the cell lysate under constant mixing for 10 min – 2 h at room temperature or 4°C.
    note: during incubation of protein sample with the GFP-Trap®_A the final concentration of detergents should not exceed 0.2% to avoid unspecific binding to the matrix
  • 7. Spin tube at 2.500x g for 2 minutes at 4°C. For western blot analysis dilute 50 µL supernatant with 50 µL 2x SDS-sample buffer (à refer to as non-bound). Discard remaining supernatant.
  • 8. Wash beads three times with 500 µL ice cold wash buffer. After the last wash step, transfer beads to new tube.
    optional: increase salt concentration in the second washing step up to 500 mM
  • 9. Resuspend GFP-Trap®_A beads in 100 µL 2x SDS-Sample buffer or go to step 11.
  • 10. Boil resuspended beads for 10 minutes at 95°C to dissociate the immunocomplexes from the beads. The beads can be collected by centrifugation at 2.500x g for 2 minutes at 4°C and SDS-PAGE is performed with the supernatant (à refer to as bound).
  • 11. optional: elute bound proteins by adding 50 µL 0.2 M glycine pH 2.5 (incubation time: 30 sec under constant mixing) followed by centrifugation. Transfer the supernatant to a fresh cup and add 5 µL 1M Tris base (pH 10.4) for neutralization. To increase elution efficiency this step can be repeated.
Restrictions For Research Use only
Concentration 500 µL resin
Buffer 20% EtOH
Handling Advice Do not freeze.
Storage 4 °C/-20 °C
Storage Comment GFP-Trap® is extremely stable (up to 70°C, functional in 2M NaCl or 0.5% SDS) and has a high affinity binding (dissociation constant in the sub-nanomolar range).
Expiry Date 12 months
Supplier Images
GFP-Trap® A Left (IP): Pulldown of GFP with GFP-Trap®_A and GFP-Trap®_M from 293T cell extracts. Input (I) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining. Right (Co-IP): Pulldown of GFP-PCNA with GFP-Trap®_A and GFP-Trap®_M from 293T cell extracts. Other bands: potential interaction partners of PCNA.
GFP-Trap® A (2) Comparison of GFP-Trap with conventional mono- and polyclonal antibodies: Immunoprecipitations (IP) of GFP from protein extracts of GFP-producing human cells. Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western Blotting. (hc) heavy chain, (lc) light chain of conventional antibodies.
Product cited in: Gunaratne, Goh, Swa et al.: "Protein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification." in: The Journal of biological chemistry, Vol. 286, Issue 20, pp. 18093-103, 2011 (PubMed). Further details: We performed one-step purification using GFP-trap

Dosil: "Ribosome synthesis-unrelated functions of the preribosomal factor rrp12 in cell cycle progression and the DNA damage response." in: Molecular and cellular biology, Vol. 31, Issue 12, pp. 2422-38, 2011 (PubMed).

Dosko?ilova?, Pla?hal, Volc et al.: "A nodulin/glutamine synthetase-like fusion protein is implicated in the regulation of root morphogenesis and in signalling triggered by flagellin." in: Planta, 2011 (PubMed). Further details: immunoprecipitation of the protein from S27 using GFP-Trap A

Walkey, Luo, Borchers et al.: "The Saccharomyces cerevisiae fermentation stress response protein Igd1p/Yfr017p regulates glycogen levels by inhibiting the glycogen debranching enzyme." in: FEMS yeast research, 2011 (PubMed).

Meruvu, Hugendubler, Mueller: "Regulation of Adipocyte Differentiation by the Zinc Finger Protein ZNF638." in: The Journal of biological chemistry, 2011 (PubMed). Further details: For GFP IP assays, transfected HEK-293 cells were lysed, 30 ?l of GFP-Trap

Nagel, Albrecht, Milovic-Holm et al.: "Herpes Simplex Virus Immediate Early Protein ICP0 is Targeted by SIAH-1 for Proteasomal Degradation." in: Journal of virology, 2011 (PubMed).

García-Gómez, Lebaron, Froment et al.: "Dynamics of the putative RNA helicase Spb4 during ribosome assembly in Saccharomyces cerevisiae." in: Molecular and cellular biology, 2011 (PubMed).

Engeland, Oberwinkler, Schümann et al.: "The cellular protein Lyric interacts with HIV-1 Gag." in: Journal of virology, 2011 (PubMed).

Doggett, Zhao, Mork et al.: "Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition." in: Journal of neurochemistry, 2011 (PubMed).

Essid, Gopaldass, Yoshida et al.: "Rab8a regulates the exocyst-mediated kiss-and-run discharge of the Dictyostelium contractile vacuole." in: Molecular biology of the cell, 2012 (PubMed).

Moulin, Anderton, Voss et al.: "IAPs limit activation of RIP kinases by TNF receptor 1 during development." in: The EMBO journal, 2012 (PubMed). Further details: GFP fusion proteins were precipitated using GFP

Dittmer, Förstemann: "Murine cytomegalovirus infection of cultured mouse cells induces expression of miR-7a." in: The Journal of general virology, Vol. 93, Issue Pt 7, pp. 1537-47, 2012 (PubMed).

Shi, Azoulay, Dingli et al.: "SNAP-tag based proteomics approach for the study of the retrograde route." in: Traffic (Copenhagen, Denmark), Vol. 13, Issue 7, pp. 914-25, 2012 (PubMed).

Dimmer, Papić, Schumann et al.: "A crucial role for Mim2 in the biogenesis of mitochondrial outer membrane proteins." in: Journal of cell science, Vol. 125, Issue Pt 14, pp. 3464-73, 2012 (PubMed).

Cai, Zhuang, Wang et al.: "Vacuolar degradation of two integral plasma membrane proteins, AtLRR84A and OsSCAMP1, is cargo ubiquitination-independent and prevacuolar compartment-mediated in plant cells." in: Traffic (Copenhagen, Denmark), Vol. 13, Issue 7, pp. 1023-40, 2012 (PubMed).

Ledri, Nikitidou, Erdelyi et al.: "Altered profile of basket cell afferent synapses in hyper-excitable dentate gyrus revealed by optogenetic and two-pathway stimulations." in: The European journal of neuroscience, Vol. 36, Issue 1, pp. 1971-83, 2012 (PubMed).

Ivanov, Fedorova, Limpens et al.: "Rhizobium-legume symbiosis shares an exocytotic pathway required for arbuscule formation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, Issue 21, pp. 8316-21, 2012 (PubMed).

Aumiller, Graebsch, Kremmer et al.: "Drosophila Pur-α binds to trinucleotide-repeat containing cellular RNAs and translocates to the early oocyte." in: RNA biology, Vol. 9, Issue 5, pp. 633-43, 2012 (PubMed).

Poulsen, Madsen, Young et al.: "Comprehensive profiling of proteome changes upon sequential deletion of deubiquitylating enzymes." in: Journal of proteomics, Vol. 75, Issue 13, pp. 3886-97, 2012 (PubMed).

Steenhuis, Froemming, Reinheckel et al.: "Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7." in: Biochimica et biophysica acta, Vol. 1822, Issue 10, pp. 1617-28, 2012 (PubMed).

Tomaštíková, Cenklová, Kohoutová et al.: "Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes." in: BMC plant biology, Vol. 12, pp. 83, 2012 (PubMed).

Alves-Silva, Sánchez-Soriano, Beaven et al.: "Spectraplakins promote microtubule-mediated axonal growth by functioning as structural microtubule-associated proteins and EB1-dependent +TIPs (tip interacting proteins)." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 32, Issue 27, pp. 9143-58, 2012 (PubMed).

Chen, Schaap: "The prokaryote messenger c-di-GMP triggers stalk cell differentiation in Dictyostelium." in: Nature, Vol. 488, Issue 7413, pp. 680-3, 2012 (PubMed).

Kraft, Kijanska, Kalie et al.: "Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy." in: The EMBO journal, Vol. 31, Issue 18, pp. 3691-703, 2012 (PubMed).

Castro-Castro, Janke, Montagnac et al.: "ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of alpha-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion." in: European journal of cell biology, 2012 (PubMed).

Buisson, Masson: "PALB2 self-interaction controls homologous recombination." in: Nucleic acids research, 2012 (PubMed).

Dingli, Parys, Loew et al.: "Vimentin and the K-Ras-induced actin-binding protein control inositol-(1,4,5)-trisphosphate receptor redistribution during MDCK cell differentiation." in: Journal of cell science, Vol. 125, Issue Pt 22, pp. 5428-40, 2013 (PubMed).

Hermanson, Carlson, Riddle et al.: "Screening for Novel LRRK2 Inhibitors Using a High-Throughput TR-FRET Cellular Assay for LRRK2 Ser935 Phosphorylation." in: PLoS ONE, Vol. 7, Issue 8, pp. e43580, 2012 (PubMed).

Magiera, Mora, Mojsa et al.: "Trim17-mediated ubiquitination and degradation of Mcl-1 initiate apoptosis in neurons." in: Cell death and differentiation, Vol. 20, Issue 2, pp. 281-92, 2013 (PubMed).

Sohn, Hughes, Piquerez et al.: "Distinct regions of the Pseudomonas syringae coiled-coil effector AvrRps4 are required for activation of immunity." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, Issue 40, pp. 16371-6, 2012 (PubMed).

Lee, Fischer: "Drosophila Tel2 is expressed as a translational fusion with EpsinR and is a regulator of wingless signaling." in: PLoS ONE, Vol. 7, Issue 9, pp. e46357, 2012 (PubMed).

Villa, Forné, Müller et al.: "MSL2 combines sensor and effector functions in homeostatic control of the Drosophila dosage compensation machinery." in: Molecular cell, Vol. 48, Issue 4, pp. 647-54, 2012 (PubMed).

Wunder, Liu, Aseeva et al.: "Control of STN7 transcript abundance and transient STN7 dimerisation are involved in the regulation of STN7 activity." in: Planta, Vol. 237, Issue 2, pp. 541-58, 2013 (PubMed).

Hagemann, Ackermann, Christmann et al.: "The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis." in: Oncogene, Vol. 32, Issue 39, pp. 4602-13, 2013 (PubMed).

Collu, Hidalgo-Sastre, Acar et al.: "Dishevelled limits Notch signalling through inhibition of CSL." in: Development (Cambridge, England), Vol. 139, Issue 23, pp. 4405-15, 2012 (PubMed).

Gamalinda, Jakovljevic, Babiano et al.: "Yeast polypeptide exit tunnel ribosomal proteins L17, L35 and L37 are necessary to recruit late-assembling factors required for 27SB pre-rRNA processing." in: Nucleic acids research, Vol. 41, Issue 3, pp. 1965-83, 2013 (PubMed).

Ohta, Schumacher, Mehellou et al.: "The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction." in: The Biochemical journal, Vol. 451, Issue 1, pp. 111-22, 2013 (PubMed).

Nicaise, Joe, Jeong et al.: "Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7." in: The EMBO journal, Vol. 32, Issue 5, pp. 701-12, 2013 (PubMed).

Watkins, Patil, Goult et al.: "A novel interaction between FRMD7 and CASK: evidence for a causal role in idiopathic infantile nystagmus." in: Human molecular genetics, Vol. 22, Issue 10, pp. 2105-18, 2013 (PubMed).

Lipchik, Parker: "Time-resolved luminescence detection of spleen tyrosine kinase activity through terbium sensitization." in: Analytical chemistry, Vol. 85, Issue 5, pp. 2582-8, 2013 (PubMed).

Doskočilová, Kohoutová, Volc et al.: "NITRILASE1 regulates the exit from proliferation, genome stability and plant development." in: The New phytologist, Vol. 198, Issue 3, pp. 685-98, 2013 (PubMed).

Wirth, Karaca, Wenzel et al.: "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases." in: Mitochondrion, Vol. 13, Issue 6, pp. 705-20, 2013 (PubMed).

Maemoto, Kiso, Shibata et al.: "Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells." in: The FEBS journal, 2013 (PubMed).

Elias, Wu, Chen: "Tumor Suppressor Protein p53 Negatively Regulates Human Pregnane X Receptor Activity." in: Molecular pharmacology, 2013 (PubMed).

Stam, Jupe, Howden et al.: "Identification and Characterisation CRN Effectors in Phytophthora capsici Shows Modularity and Functional Diversity." in: PLoS ONE, Vol. 8, Issue 3, pp. e59517, 2013 (PubMed).

Convertini, Zhang, de la Grange et al.: "Genome wide array analysis indicates that an amyotrophic lateral sclerosis mutation of FUS causes an early increase of CAMK2N2 in vitro." in: Biochimica et biophysica acta, 2013 (PubMed).

Neukamm, Ott, Dammeier et al.: "Phosphorylation of serine 1137/1138 of mouse insulin receptor substrate (IRS) 2 regulates cAMP-dependent binding to 14-3-3 proteins and IRS2 protein degradation." in: The Journal of biological chemistry, Vol. 288, Issue 23, pp. 16403-15, 2013 (PubMed).

Moreno, Shyu, Campos et al.: "Negative Feedback Control of Jasmonate Signaling by an Alternative Splice Variant of JAZ10." in: Plant physiology, 2013 (PubMed).

Ono, Yamada, Endo et al.: "Analysis of human protein replacement stable cell lines established using snoMEN-PR vector." in: PLoS ONE, Vol. 8, Issue 4, pp. e62305, 2013 (PubMed).

Stockert, Wolf, Kaddatz et al.: "Regulation of TAK1/TAB1-mediated IL-1? signaling by cytoplasmic PPAR?/?." in: PLoS ONE, Vol. 8, Issue 4, pp. e63011, 2013 (PubMed).

Fei, Yu, Geahlen: "Modulation by Syk of Bcl-2, calcium and the calpain-calpastatin proteolytic system in human breast cancer cells." in: Biochimica et biophysica acta, Vol. 1833, Issue 10, pp. 2153-64, 2013 (PubMed).

Kim, Chiang, Kieber et al.: "SCF(KMD) controls cytokinin signaling by regulating the degradation of type-B response regulators." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, Issue 24, pp. 10028-33, 2013 (PubMed).

Petherick, Williams, Lane et al.: "Autolysosomal β-catenin degradation regulates Wnt-autophagy-p62 crosstalk." in: The EMBO journal, Vol. 32, Issue 13, pp. 1903-16, 2013 (PubMed).

Lundby, Andersen, Steffensen et al.: "In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling." in: Science signaling, Vol. 6, Issue 278, pp. rs11, 2013 (PubMed).

Shen, Suen, Wang et al.: "An in vivo expression system for the identification of cargo proteins of vacuolar sorting receptors in Arabidopsis culture cells." in: The Plant journal : for cell and molecular biology, Vol. 75, Issue 6, pp. 1003-17, 2013 (PubMed).

Poulsen, Hansen, Wagner et al.: "RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response." in: The Journal of cell biology, Vol. 201, Issue 6, pp. 797-807, 2013 (PubMed).

Derkacheva, Steinbach, Wildhaber et al.: "Arabidopsis MSI1 connects LHP1 to PRC2 complexes." in: The EMBO journal, Vol. 32, Issue 14, pp. 2073-85, 2013 (PubMed).

Popichenko, Hugosson, Sjögren et al.: "Jeb/Alk signalling regulates the Lame duck GLI family transcription factor in the Drosophila visceral mesoderm." in: Development (Cambridge, England), Vol. 140, Issue 15, pp. 3156-66, 2013 (PubMed).

Sun, Li, Suo et al.: "Global analysis of fission yeast mating genes reveals new autophagy factors." in: PLoS genetics, Vol. 9, Issue 8, pp. e1003715, 2013 (PubMed).

Vanderperre, Lucier, Bissonnette et al.: "Direct detection of alternative open reading frames translation products in human significantly expands the proteome." in: PLoS ONE, Vol. 8, Issue 8, pp. e70698, 2013 (PubMed).

Berk, Maitra, Dawdy et al.: "O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched \"." in: The Journal of biological chemistry, Vol. 288, Issue 42, pp. 30192-209, 2013 (PubMed).

Amsalem, Bakrhat, Otani et al.: "Drosophila oocyte polarity and cytoskeleton organization require regulation of ik2 activity by spn-f and javelin-like." in: Molecular and cellular biology, Vol. 33, Issue 22, pp. 4371-80, 2013 (PubMed).

Rametta, Nebbia, Dongiovanni et al.: "A novel alpha1-antitrypsin null variant (PiQ0Milano )." in: World journal of hepatology, Vol. 5, Issue 8, pp. 458-61, 2013 (PubMed).

Aich, Shaha: "Novel role of calmodulin in regulating protein transport to mitochondria in a unicellular eukaryote." in: Molecular and cellular biology, Vol. 33, Issue 22, pp. 4579-93, 2013 (PubMed).

Kirkwood, Ahmad, Larance et al.: "Characterisation of Native Protein Complexes and Protein Isoform Variation using Size-Fractionation Based Quantitative Proteomics." in: Molecular & cellular proteomics : MCP, 2013 (PubMed).

Köster, Staiger: "RNA-binding protein immunoprecipitation from whole-cell extracts." in: Methods in molecular biology (Clifton, N.J.), Vol. 1062, pp. 679-95, 2013 (PubMed).

Kelsall, Duda, Olszewski et al.: "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes." in: The EMBO journal, Vol. 32, Issue 21, pp. 2848-60, 2013 (PubMed).

Sasaki-Osugi, Imoto, Takahara et al.: "Nuclear ALG-2 Protein Interacts with Ca2+ Homeostasis Endoplasmic Reticulum Protein (CHERP) Ca2+-dependently and Participates in Regulation of Alternative Splicing of Inositol Trisphosphate Receptor Type 1 (IP3R1) Pre-mRNA." in: The Journal of biological chemistry, Vol. 288, Issue 46, pp. 33361-75, 2013 (PubMed).

Lai, Tan, Gunaratne et al.: "Localization of HPV-18 E2 at Mitochondrial Membranes Induces ROS Release and Modulates Host Cell Metabolism." in: PLoS ONE, Vol. 8, Issue 9, pp. e75625, 2013 (PubMed).

Baierlein, Hackmann, Gross et al.: "Monosome Formation during Translation Initiation Requires the SR Protein Npl3." in: Molecular and cellular biology, 2013 (PubMed).

Villumsen, Danielsen, Povlsen et al.: "A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis." in: The EMBO journal, 2013 (PubMed).

Stathopoulou, Cuello, Candasamy et al.: "Four-and-a-half LIM domains proteins are novel regulators of the protein kinase D pathway in cardiac myocytes." in: The Biochemical journal, 2013 (PubMed).

Xu, Ball, Chen et al.: "The Yeast Shu Complex Utilizes Homologous Recombination Machinery for Error-free Lesion Bypass via Physical Interaction with a Rad51 Paralogue." in: PLoS ONE, Vol. 8, Issue 12, pp. e81371, 2013 (PubMed).

Meijer, Hua, Kots et al.: "Actin dynamics in Phytophthora infestans; rapidly reorganizing cables and immobile, long-lived plaques." in: Cellular microbiology, 2014 (PubMed).

Li, Sun, Williams et al.: "Identification of the self-incompatibility locus F-box protein-containing complex in Petunia inflata." in: Plant reproduction, 2014 (PubMed).

Spallek, Beck, Ben Khaled et al.: "ESCRT-I Mediates FLS2 Endosomal Sorting and Plant Immunity." in: PLoS genetics, Vol. 9, Issue 12, pp. e1004035, 2014 (PubMed).

Daou, Hasan, Breitsprecher et al.: "Essential and non-redundant roles for Diaphanous formins in cortical microtubule capture and directed cell migration." in: Molecular biology of the cell, 2014 (PubMed).

Han, Gambin, Gomez et al.: "Cortactin scaffolds Arp2/3 and WAVE2 at the epithelial zonula adherens." in: The Journal of biological chemistry, 2014 (PubMed).

Tinti, Madeira, Murugesan et al.: "ANIA: ANnotation and Integrated Analysis of the 14-3-3 interactome." in: Database : the journal of biological databases and curation, Vol. 2014, pp. bat085, 2014 (PubMed).

LaConte, Chavan, Mukherjee: "Identification and glycerol-induced correction of misfolding mutations in the X-linked mental retardation gene CASK." in: PLoS ONE, Vol. 9, Issue 2, pp. e88276, 2014 (PubMed).

Wang, Liu, Dou et al.: "Mitotic Regulator Mis18β Interacts with and Specifies the Centromeric Assembly of Molecular Chaperone Holliday Junction Recognition Protein (HJURP)." in: The Journal of biological chemistry, Vol. 289, Issue 12, pp. 8326-36, 2014 (PubMed).

Sylvestersen, Horn, Jungmichel et al.: "Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest." in: Molecular & cellular proteomics : MCP, 2014 (PubMed).

Storm, Kumpfmueller, Bone et al.: "Zscan4 Is Regulated by PI3-Kinase and DNA-Damaging Agents and Directly Interacts with the Transcriptional Repressors LSD1 and CtBP2 in Mouse Embryonic Stem Cells." in: PLoS ONE, Vol. 9, Issue 3, pp. e89821, 2014 (PubMed).

Piquerez, Balmuth, Sklenář et al.: "Identification of post-translational modifications of plant protein complexes." in: Journal of visualized experiments : JoVE, Issue 84, pp. e51095, 2014 (PubMed).

Wilson, Leszczynska, Poulter et al.: "RhoJ interacts with the GIT-PIX complex and regulates focal adhesion disassembly." in: Journal of cell science, Vol. 127, Issue Pt 14, pp. 3039-51, 2014 (PubMed).

Jafferali, Vijayaraghavan, Figueroa et al.: "MCLIP, an effective method to detect interactions of transmembrane proteins of the nuclear envelope in live cells." in: Biochimica et biophysica acta, Vol. 1838, Issue 10, pp. 2399-2403, 2014 (PubMed).

Reynolds, Doggett, Riddle et al.: "LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status." in: Frontiers in molecular neuroscience, Vol. 7, pp. 54, 2014 (PubMed).

Du, Ma, Meruvu et al.: "The adipogenic transcriptional cofactor ZNF638 interacts with splicing regulators and influences alternative splicing." in: Journal of lipid research, 2014 (PubMed).

Wang, Childress, Geahlen: "Syk interacts with and phosphorylates nucleolin to stabilize Bcl-xL mRNA and promote cell survival." in: Molecular and cellular biology, 2014 (PubMed).

General Rothbauer, Zolghadr, Tillib et al.: "Targeting and tracing antigens in live cells with fluorescent nanobodies." in: Nature methods, Vol. 3, Issue 11, pp. 887-9, 2006 (PubMed).

Agarwal, Hardt, Brero et al.: "MeCP2 interacts with HP1 and modulates its heterochromatin association during myogenic differentiation." in: Nucleic acids research, Vol. 35, Issue 16, pp. 5402-8, 2007 (PubMed).

Rothbauer, Zolghadr, Muyldermans et al.: "A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins." in: Molecular & cellular proteomics : MCP, Vol. 7, Issue 2, pp. 282-9, 2008 (PubMed).

Trinkle-Mulcahy, Boulon, Lam et al.: "Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes." in: The Journal of cell biology, Vol. 183, Issue 2, pp. 223-39, 2008 (PubMed).

Maerz, Dettmann, Seiler: "Hydrophobic Motif Phosphorylation Coordinates Activity and Polar Localization of the Neurospora crassa Nuclear Dbf2-Related Kinase COT1." in: Molecular and cellular biology, Vol. 32, Issue 11, pp. 2083-98, 2012 (PubMed).

Tan, Gunaratne, Lai et al.: "HPV-18 E2^E4 chimera: 2 new spliced transcripts and proteins induced by keratinocyte differentiation." in: Virology, Vol. 429, Issue 1, pp. 47-56, 2012 (PubMed).

Cho, Stevens, Sieverman et al.: "A ventrally localized protease in the Drosophila egg controls embryo dorsoventral polarity." in: Current biology : CB, Vol. 22, Issue 11, pp. 1013-8, 2012 (PubMed).

Wu, Tran, Teng et al.: "The interactome of the human respiratory syncytial virus NS1 protein interactome highlights multiple effects on host cell biology." in: Journal of virology, 2012 (PubMed).

Park, Touihri, Müller et al.: "Sec1/Munc18 protein stabilizes fusion-competent syntaxin for membrane fusion in Arabidopsis cytokinesis." in: Developmental cell, Vol. 22, Issue 5, pp. 989-1000, 2012 (PubMed).

Okada, Uezu, Soderblom et al.: "Peptide Array X-Linking (PAX): A New Peptide-Protein Identification Approach." in: PLoS ONE, Vol. 7, Issue 5, pp. e37035, 2012 (PubMed).

Validation Images
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