VASP
Reactivité: Humain
WB, IHC, ELISA
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
WB: 1:500~1:1000.
Restrictions
For Research Use only
Format
Liquid
Concentration
100ug/100ul.
Buffer
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 50% glycerol
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C
Millard, Bompard, Heung, Dafforn, Scott, Machesky, Fütterer: "Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53." dans: The EMBO journal, Vol. 24, Issue 2, pp. 240-50, (2005) (PubMed).
Kühnel, Jarchau, Wolf, Schlichting, Walter, Wittinghofer, Strelkov: "The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 49, pp. 17027-32, (2004) (PubMed).
Zhao, Jiang, Kroll, Huber: "A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization." dans: The EMBO journal, Vol. 20, Issue 9, pp. 2315-25, (2001) (PubMed).
Ramesh, Antón, Hartwig, Geha: "WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 26, pp. 14671-6, (1998) (PubMed).
Haffner, Jarchau, Reinhard, Hoppe, Lohmann, Walter: "Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP." dans: The EMBO journal, Vol. 14, Issue 1, pp. 19-27, (1995) (PubMed).