GFP-Trap®

Details for Product No. ABIN509407, Supplier: Log in to see
Antigen
  • green fluorescent protein
  • gfp
Reactivity
Aequorea victoria
11
Host
Camelidae
Antibody Type
Recombinant Antibody
Application
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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Purpose For biochemical analyses of GFP fusion proteins.
Brand GFP-Trap®
Sample Type Cell Extracts
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.
Purification Purified protein
Components GFP-Trap® uncoupled
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.
Assay Time 1.5 h
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)
Restrictions For Research Use only
Format Liquid
Concentration 250 µL resin (1mg/mL)
Buffer 1 x PBS,0.01% Sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Do not freeze.
Storage 4 °C
Expiry Date 12 months
Supplier Images
 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...
Product cited 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).

Xiao, MacNair, McGoldrick, McKeever, McLean, Zhang, Keith, Zinman, Rogaeva, Robertson: "Isoform Specific Antibodies Reveal Distinct Subcellular Localizations of C9orf72 in Amyotrophic Lateral Sclerosis." in: Annals of neurology, 2015 (PubMed).

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).

Hyodo, Taniguchi, Manabe, Kaido, Mise, Sugawara, Taniguchi, Okuno: "Phosphatidic acid produced by phospholipase D promotes RNA replication of a plant RNA virus." in: PLoS pathogens, Vol. 11, Issue 5, pp. e1004909, 2015 (PubMed).

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).

Verheyen, Görnemann, Verbinnen, Boens, Beullens, Van Eynde, Bollen: "Genome-wide promoter binding profiling of protein phosphatase-1 and its major nuclear targeting subunits." in: Nucleic acids research, Vol. 43, Issue 12, pp. 5771-84, 2015 (PubMed).

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).

Frey, Lahmann, Hartmann, Seiler, Pöggeler: "Deletion of Smgpi1 encoding a GPI-anchored protein suppresses sterility of the STRIPAK mutant ΔSmmob3 in the filamentous ascomycete Sordaria macrospora." in: Molecular microbiology, Vol. 97, Issue 4, pp. 676-97, 2015 (PubMed).

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).