Girdin Antibody

INQUIRY

CAT. NO.: AMA-0257

Target Information
UniProt ID	Q3V6T2

Product Details
Size	100 µL
Reactivity	Human
Storage	Store at -20°C. Do not aliquot the antibody.
Purification	Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu1451 of human girdin protein. Antibodies are purified by protein A and peptide affinity chromatography.

Usage
Application	WB, IP
Product Usage Information Dilution	Western Blotting (1:1000); Immunoprecipitation (1:100)
MW (Target)	220-250 kDa

Background
The actin-binding protein girdin (CCDC88A, GIV) is a non-receptor guanine nucleotide exchange factor (GEF) and part of a scaffold that mediates key signaling pathways during cell migration. Girdin protein structure includes an amino-terminal Hook domain for microtubule interaction, a coiled-coil dimerization domain, a Gα binding domain, a PI(4)P-binding domain, and a carboxy-terminal receptor-binding domain within a GEF motif. Akt kinase phosphorylates girdin at Ser1416, which promotes PI(4)P binding, localization of girdin to the membrane leading edge, and regulation of actin organization and cell motility. After growth factor receptor activation, girdin binds both G-protein and receptor to form an activation complex at the receptor cytoplasmic tail. The activation complex enhances receptor autophosphorylation and promotes downstream signaling that results in actin organization and cell migration. An activated growth factor phosphorylates girdin at its carboxy-terminal Tyr1764 and Tyr1798 residues to form an SH2 docking site for PI3K binding. The girdin GEF motif interacts with Gα and leads to release of Gβγ, resulting in further PI3K activation and the completion of signal transduction from receptor to cytoskeleton. The cytoskeletal reorganization and cell migration properties of girdin are important in regulating several biological processes, including wound healing, angiogenesis, and cancer progression.

Background

The actin-binding protein girdin (CCDC88A, GIV) is a non-receptor guanine nucleotide exchange factor (GEF) and part of a scaffold that mediates key signaling pathways during cell migration. Girdin protein structure includes an amino-terminal Hook domain for microtubule interaction, a coiled-coil dimerization domain, a Gα binding domain, a PI(4)P-binding domain, and a carboxy-terminal receptor-binding domain within a GEF motif. Akt kinase phosphorylates girdin at Ser1416, which promotes PI(4)P binding, localization of girdin to the membrane leading edge, and regulation of actin organization and cell motility. After growth factor receptor activation, girdin binds both G-protein and receptor to form an activation complex at the receptor cytoplasmic tail. The activation complex enhances receptor autophosphorylation and promotes downstream signaling that results in actin organization and cell migration. An activated growth factor phosphorylates girdin at its carboxy-terminal Tyr1764 and Tyr1798 residues to form an SH2 docking site for PI3K binding. The girdin GEF motif interacts with Gα and leads to release of Gβγ, resulting in further PI3K activation and the completion of signal transduction from receptor to cytoskeleton. The cytoskeletal reorganization and cell migration properties of girdin are important in regulating several biological processes, including wound healing, angiogenesis, and cancer progression.

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