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ImmunohistochemistryAntibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
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- Product number
- ABIN967237 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Vasodilator-Stimulated phosphoprotein (VASP) (pSer157) antibody
- Antibody type
- Polyclonal
- Antigen
- The antiserum was produced against synthesized phosphopeptide derived from human VASP around the phosphorylation site of serine 157 (R-V-SP-N-A).
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using nonphosphopeptide corresponding to the phosphorylation site.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- pSer157
- Vial size
- 100 μg
- Concentration
- 100ug/100ul.
- Storage
- -20°C
Submitted references Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53.
The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization.
WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells.
Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP.
Millard TH, Bompard G, Heung MY, Dafforn TR, Scott DJ, Machesky LM, Fütterer K
The EMBO journal 2005 Jan 26;24(2):240-50
The EMBO journal 2005 Jan 26;24(2):240-50
The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
Kühnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV
Proceedings of the National Academy of Sciences of the United States of America 2004 Dec 7;101(49):17027-32
Proceedings of the National Academy of Sciences of the United States of America 2004 Dec 7;101(49):17027-32
A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization.
Zhao WM, Jiang C, Kroll TT, Huber PW
The EMBO journal 2001 May 1;20(9):2315-25
The EMBO journal 2001 May 1;20(9):2315-25
WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells.
Ramesh N, Antón IM, Hartwig JH, Geha RS
Proceedings of the National Academy of Sciences of the United States of America 1997 Dec 23;94(26):14671-6
Proceedings of the National Academy of Sciences of the United States of America 1997 Dec 23;94(26):14671-6
Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP.
Haffner C, Jarchau T, Reinhard M, Hoppe J, Lohmann SM, Walter U
The EMBO journal 1995 Jan 3;14(1):19-27
The EMBO journal 1995 Jan 3;14(1):19-27
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