|Human, Monkey, Mouse, Rat|
Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting
Background: Rab7 and Rab9 are members of the Ras superfamily of small Rab GTPases (1). Both proteins are located in late endosomes, but exert different functions. Rab7 associates with the RIPL effector protein to control membrane trafficking from early to late endosome and to lysosomes (2,3). Rab7 also helps to regulate growth receptor endocytic trafficking and degradation (3,4), and maturation of phagosome and autophagic vacuoles (4-6). Rab9 interacts with its effector proteins p40 and TIP47 (7,8) to promote the MPR (mannose 6-phosphate receptor)-associated lysosomal enzyme transport between late endosomes and the trans Golgi network (9,10).
|Human, Monkey, Mouse, Rat|
Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Peptide ELISA (DELFIA), Western Blotting
Background: The ezrin, radixin, and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling, and microvilli formation (1). ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers (2). Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin) disrupts the amino- and carboxy-terminal association and may play a key role in regulating ERM protein conformation and function (3,4). Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogene-induced transformation (5). Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation (6).
Application Methods: Immunohistochemistry (Paraffin), Western Blotting
Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 3 (VAMP3), also known as cellubrevin, has a broad tissue distribution and localizes to endosomal compartments (3). VAMP3 interacts with the t-SNAREs syntaxin1, syntaxin4, SNAP23, and SNAP25 (4,5). Research studies indicate that VAMP3 is involved in transferrin receptor recycling to the plasma membrane (6) and in T-cell receptor recycling to immunological synapses (7). Inhibition of VAMP3 with tetanus toxin impairs membrane trafficking during cell migration (8).