The gene AGAP2 (ArfGAP with GTPase domain, ankyrin repeat and PH domain 2) belongs to the group of proteins called AZAPs that contain a catalytic core of PH (pleckstrin homology), Arf GAP and two or more ankyrin repeat domains. The AZAP family is further divided into four subfamilies, of which AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats. Agap2 is found to be overexpressed in various human cancers.
Immunogen
Peptide with sequence CQASLDSIREAVINSQ, from the internal region of the protein sequence according to NP_055585.1.
Biochem/physiol Actions
The gene AGAP2 (ArfGAP with GTPase domain, ankyrin repeat and PH domain 2) encodes an Arf GAP (GTPase activating protein) that catalyzes the hydrolysis of GTP bound to Arf (ADP-ribosylation factors). The AGAPs are involved in the regulation of membrane trafficking and remodeling of the actin cytoskeleton. AGAP2 is found to associate with the clathrin adaptor protein AP-1 (activator protein 1) and participate in endosomal trafficking that is dependent on AP-1/Rab4 (RAS-related GTP-binding protein). It is also involved in facilitating the invasion of glioblastoma cells. Agap2 interacts with FAK (focal adhesion kinase) to form a complex and increase its activity, thereby promoting focal adhesion disassembly, resulting in increased cell migration.
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Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.
The relevance of minor transcription start sites in broad promoters is not well understood. We have studied AGAP2 expression in prostate cancer and chronic myeloid leukemia (CML), showing transcription is initiated from alternative transcription start sites (TSSs) within a single
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