Polyglutamylation Antikörper

Produktnummer ABIN1169176

Dieses Maus Monoklonal-Antikörper erkennt spezifisch in ICC, IP, WB und IEM. Er zeigt eine Reaktivität gegenüber Alle Spezies und wurde in 31+ Publikationen erwähnt.

Kurzübersicht für Polyglutamylation Antikörper (ABIN1169176)

Target: Polyglutamylation

Reaktivität: Alle Spezies

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Unkonjugiert

Applikation: Immunocytochemistry (ICC), Immunoprecipitation (IP), Western Blotting (WB), Immunoelectron Microscopy (IEM)

Klon: GT335

Produktdetails

Spezifität: Recognizes the posttranslational modification (poly)glutamylation on proteins. Reacts with polyglutamylated alpha- and beta-tubulin.

Kreuzreaktivität: Alle Spezies

Aufreinigung: Purified from concentrated hybridoma tissue culture supernatant.

Reinheit: >95 % (SDS-PAGE)

Immunogen: Octapeptide EGEGE*EEG, modified by the addition of two glutamyl units onto the fifth E (indicated by an asterisk).

Isotyp: IgG1

Anwendungsinformationen

Applikationshinweise: Optimal working dilution should be determined by the investigator.

Kommentare:

Recognizes most forms of polyglutamylated tubulin (alpha- and beta-tubulin), independent of the length of the glutamate side chains. No specificity to particular tubulin isoforms nor to tubulin from particular species are observed. Detects also other (poly)glutamylated proteins. Since no consensus modification site is known for protein (poly)glutamylation, the detection is not sequence-specific. However, an acidic environment of the modification site is required. The use of the antibody at too high concentrations obscures its specificity in immunofluorescence.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: Lot specific

Buffer: In PBS containing 10 % glycerol and 0.02 % sodium azide.

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: 4 °C,-20 °C

Informationen zur Lagerung: Short Term Storage: +4°C
Long Term Storage: -20°C
Stable for at least 1 year after receipt when stored at -20°C.

Haltbarkeit: 12 months

Referenzen

Lara Ordónez, Fernández, Fdez, Romo-Lozano, Madero-Pérez, Lobbestael, Baekelandt, Aiastui, López de Munaín, Melrose, Civiero, Hilfiker: "RAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase-mediated centrosomal cohesion and ciliogenesis deficits." in: Human molecular genetics, Vol. 28, Issue 21, pp. 3552-3568, (2020) (PubMed).

Kunova Bosakova, Nita, Gregor, Varecha, Gudernova, Fafilek, Barta, Basheer, Abraham, Balek, Tomanova, Fialova Kucerova, Bosak, Potesil, Zieba, Song, Konik, Park, Duran, Zdrahal, Smajs, Jansen, Fu, Ko et al.: "Fibroblast growth factor receptor influences primary cilium length through an interaction with intestinal cell kinase. ..." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, Issue 10, pp. 4316-4325, (2020) (PubMed).

Olstad, Ringers, Hansen, Wens, Brandt, Wachten, Yaksi, Jurisch-Yaksi: "Ciliary Beating Compartmentalizes Cerebrospinal Fluid Flow in the Brain and Regulates Ventricular Development." in: Current biology : CB, Vol. 29, Issue 2, pp. 229-241.e6, (2020) (PubMed).

Yamamoto, Kitagawa: "Self-organization of Plk4 regulates symmetry breaking in centriole duplication." in: Nature communications, Vol. 10, Issue 1, pp. 1810, (2019) (PubMed).

de Almeida, Vieira, Paredes, Bettencourt-Dias, Barbosa-Morais: "Pan-cancer association of a centrosome amplification gene expression signature with genomic alterations and clinical outcome." in: PLoS computational biology, Vol. 15, Issue 3, pp. e1006832, (2019) (PubMed).

Watanabe, Takao, Ito, Takahashi, Kitagawa: "The Cep57-pericentrin module organizes PCM expansion and centriole engagement." in: Nature communications, Vol. 10, Issue 1, pp. 931, (2019) (PubMed).

Gilmore-Hall, Kuo, Ward, Zahra, Morrison, Perkins, La Spada: "CCP1 promotes mitochondrial fusion and motility to prevent Purkinje cell neuron loss in pcd mice." in: The Journal of cell biology, Vol. 218, Issue 1, pp. 206-219, (2019) (PubMed).

Sydor, Coyaud, Rovelli, Laurent, Liu, Raught, Mennella: "PPP1R35 is a novel centrosomal protein that regulates centriole length in concert with the microcephaly protein RTTN." in: eLife, Vol. 7, (2019) (PubMed).

Shearer, Frikstad, McKenna, McCloy, Deng, Burgess, Stokke, Patzke, Saunders: "The E3 ubiquitin ligase UBR5 regulates centriolar satellite stability and primary cilia." in: Molecular biology of the cell, Vol. 29, Issue 13, pp. 1542-1554, (2019) (PubMed).

Wang, Failler, Fu, Dynlacht: "A distal centriolar protein network controls organelle maturation and asymmetry." in: Nature communications, Vol. 9, Issue 1, pp. 3938, (2019) (PubMed).

Marteil, Guerrero, Vieira, de Almeida, Machado, Mendonça, Mesquita, Villarreal, Fonseca, Francia, Dores, Martins, Jana, Tranfield, Barbosa-Morais, Paredes, Pellman, Godinho, Bettencourt-Dias: "Over-elongation of centrioles in cancer promotes centriole amplification and chromosome missegregation." in: Nature communications, Vol. 9, Issue 1, pp. 1258, (2018) (PubMed).

OHagan, Silva, Nguyen, Zhang, Bellotti, Ramadan, Hall, Barr: "Glutamylation Regulates Transport, Specializes Function, and Sculpts the Structure of Cilia." in: Current biology : CB, Vol. 27, Issue 22, pp. 3430-3441.e6, (2018) (PubMed).

Fischer, McClements, Martinez-Fernandez de la Camara, Bellingrath, Dauletbekov, Ramsden, Hickey, Barnard, MacLaren: "Codon-Optimized RPGR Improves Stability and Efficacy of AAV8 Gene Therapy in Two Mouse Models of X-Linked Retinitis Pigmentosa." in: Molecular therapy : the journal of the American Society of Gene Therapy, Vol. 25, Issue 8, pp. 1854-1865, (2018) (PubMed).

Tsuchiya, Yoshiba, Gupta, Watanabe, Kitagawa: "Cep295 is a conserved scaffold protein required for generation of a bona fide mother centriole." in: Nature communications, Vol. 7, pp. 12567, (2018) (PubMed).

Boldt, van Reeuwijk, Lu, Koutroumpas, Nguyen, Texier, van Beersum, Horn, Willer, Mans, Dougherty, Lamers, Coene, Arts, Betts, Beyer, Bolat, Gloeckner, Haidari, Hetterschijt, Iaconis, Jenkins, Klose et al.: "An organelle-specific protein landscape identifies novel diseases and molecular mechanisms. ..." in: Nature communications, Vol. 7, pp. 11491, (2018) (PubMed).

Mahuzier, Shihavuddin, Fournier, Lansade, Faucourt, Menezes, Meunier, Garfa-Traoré, Carlier, Voituriez, Genovesio, Spassky, Delgehyr: "Ependymal cilia beating induces an actin network to protect centrioles against shear stress." in: Nature communications, Vol. 9, Issue 1, pp. 2279, (2018) (PubMed).

Hsu, Garrison, Kim, Schmitz, Searby, Zhang, Datta, Nishimura, Seo, Sheffield: "BBSome function is required for both the morphogenesis and maintenance of the photoreceptor outer segment." in: PLoS genetics, Vol. 13, Issue 10, pp. e1007057, (2017) (PubMed).

Gadadhar, Dadi, Bodakuntla, Schnitzler, Bièche, Rusconi, Janke: "Tubulin glycylation controls primary cilia length." in: The Journal of cell biology, Vol. 216, Issue 9, pp. 2701-2713, (2017) (PubMed).

Ijaz, Hatanaka, Hatanaka, Tsutsumi, Iwaki, Umemura, Ikegami, Setou: "Proper cytoskeletal architecture beneath the plasma membrane of red blood cells requires Ttll4." in: Molecular biology of the cell, Vol. 28, Issue 4, pp. 535-544, (2017) (PubMed).

Wang, Lee, Malonis, Sanchez, Dynlacht: "Tethering of an E3 ligase by PCM1 regulates the abundance of centrosomal KIAA0586/Talpid3 and promotes ciliogenesis." in: eLife, Vol. 5, (2017) (PubMed).

Antigendetails

Target: Polyglutamylation

Hintergrund: Polyglutamylation is a post-translational modification in which glutamate side chains of variable lengths are formed on the modified protein. It is evolutionarily conserved and the most prominent substrate is tubulin, the microtubule (MT) building block. Polyglutamylation has been proposed to be involved in the functional adaptation of MTs, as it occurs within the carboxy-terminal tubulin tails that participate directly in the binding of many structural and motor MT-associated proteins. The recent identification of new substrates of polyglutamylation indicates that this post-translational modification could be a potential regulator of diverse cellular processes and be involved in cell cycle and cell proliferation.