Synembrin or Ric8A from MyBioSource.com

Resistance to inhibitors of cholinesterase (Ric) 8A is a guanine nucleotide exchange factor that activates certain G protein alpha-subunits. Earlier genetic studies have put RIC-8 under uncharacterized G protein signaling pathway that regulates centrosome movements during cell division. Various components of this pathway include G protein subunits of the Galphai class, GPR or GoLoco domain-containing proteins, RGS (regulator of G protein signaling) proteins, and other accessory factors. These proteins interact to regulate microtubule pulling forces during mitotic movement of chromosomes. The nucleus and the mitochondria of eukaryotic cells, as well as the chloroplasts in plants, contain their own genome that encodes a range of proteins and nucleic acids. The mitochondrial tRNA is encoded by nucleus and is transported in to mitochondria in many species with the help of mitochondrial transport complex as described (1). RIC8A is a 21-kDa tRNA-binding component of the tRNA complex that is partly homologous to subunit UCR6b of ubiquinol-cytochrome c reductase (OX PHOS complex III). RIC8A has binding specificity for the so-called type II tRNAs which, in vitro, require stimulation by a second group of tRNAs (type I) for import across the inner mitochondrial membrane; type I tRNAs, on the other hand, are imported efficiently by themselves, but this import is inhibited by type II tRNAs. Knockdown of RIC8A leads to deficiency of mitochondrial type II and elevation of type I tRNAs in vivo (2). In the presence of ATP, both types of tRNA are transferred from their respective receptors to a third subunit, RIC9, and thence through the membrane (3). Ric8A also interacts with Adenylyl cyclase 5A to regulate its activity. The N-terminus of each individual AC usually has a unique amino acid sequence that is important for isoform-specific regulation (3). Several interacting proteins [e.g. snapin and PP2A (protein phosphatase 2A)] which bind the N-terminus of different ACs have been reported (3), suggesting that the N-terminus might function as a scaffold which selectively mediates the cross-talk between the cAMP signaling and other machinery. AC5 contains a very long N-terminus (242 amino acids) that interacts with Ric8a as binding partner of the N-terminus of AC5. Ric8a has been demonstrated to associate with many Gá proteins in mammalian cells, including Gás, Gáq, Gáo, Gái and Gái3 (4). The association of Ric8A with AC5 Nterminal region suppress the AC5 activity via a Galphai-dependent pathway. Ric-8A interacts with GDP-bound Galpha proteins, stimulates release of GDP, and forms a stable nucleotide-free transition state complex with the Galpha protein; this complex dissociates upon binding of GTP to Galpha (4). The Ric8A-selective rabbit antibodies were generated against a unique epitope on human Ric8A homolog near C-terminal end of the protein. The synthetic peptide was covalently modified to achieve desired antigenic and was conjugated to a carrier protein before used as immunogen to raise antibodies. The Ric8A antibodies are affinity purified over immobilized immunogenic peptide affinity matrix and stabilized with preservatives for long-term storage. MyBioSource provide FITC-and Biotinylated conjugates of this antibody for direct applications in IHC applications. MyBioSource also provides limited quantities of antigenic blocking peptide for immune depletion assays wide range of antibodies to protein kinases (receptor and non-receptor kinases) and kinase inhibitors. MyBioSource will also conjugate antibodies with fluorescent probes upon request at a reasonable cost