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GFP VHH, recombinant binding protein (GFP-Trap) Kit

AM, ChIP, EAA, IP, MS, Co-IP, Pull-Down, Purif Reactivity: Aequorea victoria Cell Extracts
Pubmed (934)
Catalog No. ABIN509407
Plus shipping costs $45.00
250 μL
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  • Target
    Antibody Type
    Recombinant Antibody
    single-domain Antibody (sdAb)
    • 8
    • 4
    • 1
    Aequorea victoria
    • 9
    Camelid (Camelidae)
    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)
    For biochemical analyses of GFP fusion proteins.
    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.
    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.
    Purified protein
    Alpaca anti-GFP VHH, purified unconjugated protein
    Material not included
    Lysis buffer (CoIP), 10x RIPA buffer, Dilution buffer, Wash buffer, Elution buffer
  • 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
    • 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)
    For Research Use only
  • Format
    250 µL resin (1mg/mL)
    1 x PBS,0.01% Sodium azide
    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.
    4 °C
    Expiry Date
    12 months
  • Morra, Del Carratore, Muhamadali, Horga, Halliwell, Goodacre, Breitling, Dixon: "Translation Stress Positively Regulates MscL-Dependent Excretion of Cytoplasmic Proteins." in: mBio, Vol. 9, Issue 1, 2019 (PubMed).

    Oka, van Lith, Rudolf, Tungkum, Pringle, Bulleid: "ERp18 regulates activation of ATF6α during unfolded protein response." in: The EMBO journal, Vol. 38, Issue 15, pp. e100990, 2019 (PubMed).

    Poulsen, Kampmeyer, Kriegenburg, Johansen, Hofmann, Holmberg, Hartmann-Petersen: "UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1." in: Cell stress & chaperones, Vol. 22, Issue 1, pp. 143-154, 2018 (PubMed).

    Zabinsky, Weum, Cui, Han: "RNA Binding Protein Vigilin Collaborates with miRNAs To Regulate Gene Expression for Caenorhabditis elegans Larval Development." in: G3 (Bethesda, Md.), Vol. 7, Issue 8, pp. 2511-2518, 2018 (PubMed).

    Wang, Zhong, Shuai, Song, Zhang, Han, Ling, Tang, Wang, Song: "E+ subgroup PPR protein defective kernel 36 is required for multiple mitochondrial transcripts editing and seed development in maize and Arabidopsis." in: The New phytologist, Vol. 214, Issue 4, pp. 1563-1578, 2018 (PubMed).

    Mack, Zhang, Fonslow, Yates: "The protein kinase MBK-1 contributes to lifespan extension in daf-2 mutant and germline-deficient Caenorhabditis elegans." in: Aging, Vol. 9, Issue 5, pp. 1414-1432, 2018 (PubMed).

    Saryi, Hutchinson, Al-Hejjaj, Sedelnikova, Baker, Hettema: "Pnc1 piggy-back import into peroxisomes relies on Gpd1 homodimerisation." in: Scientific reports, Vol. 7, pp. 42579, 2018 (PubMed).

    Batinovic, McHugh, Chisholm, Matthews, Liu, Dumont, Charnaud, Schneider, Gilson, de Koning-Ward, Dixon, Tilley: "An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes." in: Nature communications, Vol. 8, pp. 16044, 2018 (PubMed).

    MacLennan, García-Cañadas, Reichmann, Khazina, Wagner, Playfoot, Salvador-Palomeque, Mann, Peressini, Sanchez, Dobie, Read, Hung, Eskeland, Meehan, Weichenrieder, García-Pérez, Adams: "Mobilization of LINE-1 retrotransposons is restricted by Tex19.1 in mouse embryonic stem cells." in: eLife, Vol. 6, 2018 (PubMed).

    Stumpf, Müller, Gaßen, Wehrstedt, Fey, Karow, Eichinger, Glöckner, Noegel: "A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium." in: Disease models & mechanisms, Vol. 10, Issue 7, pp. 897-907, 2018 (PubMed).

    Advani, Lim, Catimel, Lio, Ng, Chüeh, Tran, Anasir, Verkade, Zhu, Turk, Smithgall, Ang, Griffin, Cheng: "Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine." in: Cell communication and signaling : CCS, Vol. 15, Issue 1, pp. 29, 2018 (PubMed).

    Tang, Leung, Saturno, Viros, Smith, Di Leva, Morrison, Niculescu-Duvaz, Lopes, Johnson, Dhomen, Springer, Marais: "Lysyl oxidase drives tumour progression by trapping EGF receptors at the cell surface." in: Nature communications, Vol. 8, pp. 14909, 2018 (PubMed).

    Pawellek, Ryder, Tammsalu, King, Kreinin, Ly, Hay, Hartley, Lamond: "Characterisation of the biflavonoid hinokiflavone as a pre-mRNA splicing modulator that inhibits SENP." in: eLife, Vol. 6, 2018 (PubMed).

    Feeley, Pilla-Moffett, Zwack, Piro, Finethy, Kolb, Martinez, Brodsky, Coers: "Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 114, Issue 9, pp. E1698-E1706, 2018 (PubMed).

    Sherry, Hay, Gulak, Nassiri, Finnen, Banfield: "The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding." in: Scientific reports, Vol. 7, Issue 1, pp. 1882, 2018 (PubMed).

    King, Thillai, Whale, Arumugam, Eldaly, Kocher, Wells: "PAK4 interacts with p85 alpha: implications for pancreatic cancer cell migration." in: Scientific reports, Vol. 7, pp. 42575, 2018 (PubMed).

    Lopez-Guerrero, Tomas-Martin, Pascual-Caro, Macartney, Rojas-Fernandez, Ball, Alessi, Pozo-Guisado, Martin-Romero: "Regulation of membrane ruffling by polarized STIM1 and ORAI1 in cortactin-rich domains." in: Scientific reports, Vol. 7, Issue 1, pp. 383, 2018 (PubMed).

    Dogliotti, Kullmann, Dhumale, Thiele, Panichkina, Mendl, Houben, Haferkamp, Püschel, Krahn: "Membrane-binding and activation of LKB1 by phosphatidic acid is essential for development and tumour suppression." in: Nature communications, Vol. 8, pp. 15747, 2018 (PubMed).

    Rogov, Stolz, Ravichandran, Rios-Szwed, Suzuki, Kniss, Löhr, Wakatsuki, Dötsch, Dikic, Dobson, McEwan: "Structural and functional analysis of the GABARAP interaction motif (GIM)." in: EMBO reports, Vol. 18, Issue 8, pp. 1382-1396, 2018 (PubMed).

    Zhang, Kruse, López-Méndez, Sylvestersen, Garvanska, Schopper, Nielsen, Nilsson: "Bub1 positions Mad1 close to KNL1 MELT repeats to promote checkpoint signalling." in: Nature communications, Vol. 8, pp. 15822, 2018 (PubMed).

  • Target
    Alternative Name
    green fluorescent protein, gfp
    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 .
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