Details zu Produkt Nr. ABIN509407, Anbieter: Anmelden zum Anzeigen
  • green fluorescent protein
  • gfp
Aequorea victoria
Camelid (Camelidae)
Recombinant Antibody
Affinity Measurement (AM), Chromatin Immunoprecipitation (ChIP), Enzyme Activity Assay (EAA), Immunoprecipitation (IP), Mass Spectrometry (MS), Protein Complex Immunoprecipitation (Co-IP), Pull-Down Assay (Pull-Down), Purification (Purif)
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Hersteller Produkt- Nr.
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Verwendungszweck For biochemical analyses of GFP fusion proteins.
Marke GFP-Trap®
Proben Cell Extracts
Kreuzreaktivität (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.
Produktmerkmale 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.
Reinigung Purified protein
Bestandteile GFP-Trap® uncoupled
Benötigtes Material Lysis buffer (CoIP), 10x RIPA buffer, Dilution buffer, Wash buffer, Elution buffer
Andere Bezeichnung GFP
Hintergrund 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 .
Applikationshinweise 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.
Testdauer 1.5 h
  • 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)
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Konzentration 250 µL resin (1mg/mL)
Buffer 1 x PBS,0.01% Sodium azide
Konservierungsmittel Sodium azide
Vorsichtsmaßnahmen This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handhabung Do not freeze.
Lagerung 4 °C
Haltbarkeit 12 months
Bilder des Herstellers
 image for GFP-Trap® (ABIN509407) Left (IP): Pulldown of GFP with GFP-Trap®_A and GFP-Trap®_M from 293T cell extracts. ...
Western Blotting (WB) image for GFP-Trap® (ABIN509407) Comparison of GFP-Trap with conventional mono- and polyclonal antibodies: Immunopreci...
Produkt verwendet in: Yan, Chu, Qin, Wang, Liu, Jin, Zhang, Gomez, Hergovich, Chen, He, Gao, Yao: "Regulation of NDR1 activity by PLK1 ensures proper spindle orientation in mitosis." in: Scientific reports, Vol. 5, pp. 10449, 2015 (PubMed).

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Satpathy, Wagner, Beli, Gupta, Kristiansen, Malinova, Francavilla, Tolar, Bishop, Hostager, Choudhary: "Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation." in: Molecular systems biology, Vol. 11, Issue 6, pp. 810, 2015 (PubMed).

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Vardabasso, Gaspar-Maia, Hasson, Pünzeler, Valle-Garcia, Straub, Keilhauer, Strub, Dong, Panda, Chung, Yao, Singh, Segura, Fontanals-Cirera, Verma, Mann, Hernando, Hake, Bernstein: "Histone Variant H2A.Z.2 Mediates Proliferation and Drug Sensitivity of Malignant Melanoma." in: Molecular cell, Vol. 59, Issue 1, pp. 75-88, 2015 (PubMed).

Mochida, Oikawa, Kimura, Kirisako, Hirano, Ohsumi, Nakatogawa: "Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus." in: Nature, Vol. 522, Issue 7556, pp. 359-62, 2015 (PubMed).

Voit, Seiler, Grummt: "Cooperative Action of Cdk1/cyclin B and SIRT1 Is Required for Mitotic Repression of rRNA Synthesis." in: PLoS genetics, Vol. 11, Issue 5, pp. e1005246, 2015 (PubMed).

Van Itallie, Tietgens, Krystofiak, Kachar, Anderson: "A complex of ZO-1 and the BAR-domain protein TOCA-1 regulates actin assembly at the tight junction." in: Molecular biology of the cell, Vol. 26, Issue 15, pp. 2769-87, 2015 (PubMed).

Ojeda, Robles-Valero, Barreira, Bustelo: "The disease-linked Glu-26-Lys mutant version of Coronin 1A exhibits pleiotropic and pathway-specific signaling defects." in: Molecular biology of the cell, Vol. 26, Issue 16, pp. 2895-912, 2015 (PubMed).

Catinot, Huang, Huang, Tseng, Chen, Gu, Lo, Wang, Chen, Zimmerli: "ETHYLENE RESPONSE FACTOR 96 positively regulates Arabidopsis resistance to necrotrophic pathogens by direct binding to GCC elements of jasmonate - and ethylene-responsive defence genes." in: Plant, cell & environment, 2015 (PubMed).

Avila, Lee, Torii: "Co-Immunoprecipitation of Membrane-Bound Receptors." in: The Arabidopsis book / American Society of Plant Biologists, Vol. 13, pp. e0180, 2015 (PubMed).

Maro, Gao, Olechwier, Hung, Liu, Özkan, Zhen, Shen: "MADD-4/Punctin and Neurexin Organize C. elegans GABAergic Postsynapses through Neuroligin." in: Neuron, Vol. 86, Issue 6, pp. 1420-32, 2015 (PubMed).

Reyes, Ocolotobiche, Marmisollé, Robles Luna, Borniego, Bazzini, Asurmendi, García: "Citrus psorosis virus 24K protein interacts with citrus miRNA precursors, affects their processing and subsequent miRNA accumulation and target expression." in: Molecular plant pathology, 2015 (PubMed).

Heinick, Husser, Himmler, Kirchhefer, Nunes, Schulte, Seidl, Rolfes, Dedman, Kaetzel, Gerke, Schmitz, Müller: "Annexin A4 is a novel direct regulator of adenylyl cyclase type 5." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015 (PubMed).

Wang, Cordewener, America, Shan, Bouwmeester, Govers: "Arabidopsis lectin receptor kinases LecRK-IX.1 and LecRK-IX.2 are functional analogs in regulating Phytophthora resistance and plant cell death." in: Molecular plant-microbe interactions : MPMI, 2015 (PubMed).

Sun, Li, Lu, Williams, Kao: "Pollen S-locus F-box proteins of Petunia involved in S-RNase-based self-incompatibility are themselves subject to ubiquitin-mediated degradation." in: The Plant journal : for cell and molecular biology, Vol. 83, Issue 2, pp. 213-223, 2015 (PubMed).

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Yukawa, Ikebe, Toda: "The Msd1-Wdr8-Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies." in: The Journal of cell biology, Vol. 209, Issue 4, pp. 549-62, 2015 (PubMed).

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Qin, Wolf, Liu, Link, Smets, Mastra, Forné, Pichler, Hörl, Fellinger, Spada, Bonapace, Imhof, Harz, Leonhardt: "DNA methylation requires a DNMT1 ubiquitin interacting motif (UIM) and histone ubiquitination." in: Cell research, Vol. 25, Issue 8, pp. 911-29, 2015 (PubMed).

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