Anti-Rab13 antibody produced in rabbit

Rab13 is a member of the Rab family of Ras superfamily of small guanosine triphosphatases (GTPases). Rab13 is localized to the cytoplasmic vesicles of nonpolarized cells and at tight junctions (Tjs) in polarized epithelial cells.

synthetic peptide corresponding to amino acids 46-58 of mouse Rab13, conjugated to KLH. The corresponding sequence differs by a single amino acid in human and rat Rab13.

Anti-Rab13 antibody produced in rabbit has been used in:

• immunoblotting
• immunoprecipitation
• immunofluorescence

Rab guanosine triphosphatases (GTPases) are central regulators of membrane trafficking between the different subcellular compartments of the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP-bound inactive and GTP-bound active states. Activation of a Rab protein is coupled to its association with intracellular membranes. Rab proteins contain conserved regions involved in guanine-nucleotide binding and hypervariable COOH-terminal domains with a cysteine motif, implicated in subcellular targeting. Rab13 mediates tight junctions assembly in epithelial cells by regulating cAMP dependent protein kinase (PKA) mediated phosphorylation of vasodilator stimulated phosphoprotein (VASP) and its recruitment to cell-cell junctions. Rab13 also regulates membrane trafficking between the thyroglobulin (TGN) and recycling endosomes in polarized epithelial cells during biosynthetic delivery. Each Rab protein shows a characteristic subcellular distribution. Therefore, antibodies to Rab proteins may serve as useful tools for studying subcellular localization and membrane organization.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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