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Heterotrimeric guanine nucleotide-binding proteins (G proteins) which integrate signals between receptors and effector proteins, are comprised of an alpha, a beta and a gamma subunit. The alpha, beta and gamma subunits are encoded by families of related genes. GNB1 encodes a beta subunit. Beta subunits are vital regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. G proteins are involved as a modulator or transducer in numerous transmembrane signaling systems. The beta and gamma chains are necessary for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

GNG4 belongs to a multigene family and is involved in defining the specificity of receptor-G protein interaction. In mammals, G protein alpha, beta and gamma polypeptides are encoded by no less than 16, 4 and 7 genes, respectively. It is a well-known fact that different G protein complexes expressed in different tissues carry structurally distinct members of the alpha beta and gamma subunits and that privileged connotation between members of subunit families rise G protein functional diversity.

Guanine nucleotide binding proteins are heterotrimeric signal-transducing molecules comprising alpha, beta, and gamma subunits. GNAI1 represents the alpha subunit of an inhibitory complex. Guanine nucleotide-binding protein G(i) subunit alpha (GNAI1) functions to transmit information from cell surface receptors to intracellular effectors. GNAI1 binds guanine nucleotide, can hydrolyze GTP, and can interact with other proteins. GNAI1 is part of a complex that responds to beta-adrenergic signals by inhibiting adenylate cyclase. In addition, GNAI1 functions to open atrial potassium channels.

Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.

GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

RAB1A belongs to the ras-related superfamily. Rab proteins have a central part in either in endocytosis or in biosynthetic protein transport. Rab1a protein controls vesicle traffic from the endoplasmic reticulum to the Golgi apparatus.

RHOC is a small signaling G protein/GTPase which is part of the Rac subfamily of the family Rho family of GTPases. RHOC rotats between inactive GDP-bound and active GTP-bound states and has a role as a molecular switch in signal transduction cascades. RHOC promotes reorganization of the actin cytoskeleton and regulates cell shape, attachment, and motility.

Guanine Nucleotide Binding Protein Gamma 11 (GNG11) which belongs to the guanine nucleotide-binding protein (G protein) gamma family encodes a lipid-anchored, cell membrane protein. G proteins act as a modulator or transducer in various transmembrane signaling systems. GNG11 is also subject to carboxyl-terminal processing.

RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.

Myxoma Resistance Protein 1 (MX1) is a member of the dynamin family and contains 1 GED domain. MX1 is an Interferon-induced dynamin-like GTPase with antiviral activity against rabies virus (RABV), vesicular stomatitis virus (VSV) and murine pneumonia virus (MPV). MX1 is ubiquitously expressed. MX1 is induced by type I and type III interferons.

Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

GH receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, GH performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

GNAI3 is a member of the G-alpha family and G (i/o/t/z) subfamily which act as modulators or transducers in several transmembrane signaling systems. G(k) is the stimulatory G protein of receptor-regulated K+ channels. The active GTP-bound form inhibits the connotation of RGS14 with centrosomes and is essential for the translocation of RGS14 from the cytoplasm to the plasma membrane. GNAI3 takes part in cell division and is known to cooperate with RIC8A, S1PR1, RGS5, RGS10, RGS12, RGS14, RGS16, RGS18, and RGS19.

RAB10, Member RAS Oncogene Family (RAB10) belongs to the Ras superfamily of small GTP-binding proteins. RAB10 is a key regulator of endocytic recycling, particularly in the basolateral recycling pathways of polarized epithelial cells. It is required for the recruitment of CNT-1 to endosomal membranes in the intestinal epithelium.

Guanine Nucleotide Binding Protein Gamma 13, also known as GNG13 is a member of the G protein gamma family. Heterotrimeric G proteins, which consist of alpha, beta, and gamma subunits, function as signal transducers for the 7-transmembrane-helix G protein-coupled receptors. GNG13 is the gamma subunit which is expressed in taste, retinal, and neuronal tissues and takes a central part in taste transduction.

RAB14 belongs to the RAB protein family, low molecular mass monomeric GTPases which is found on the cytoplasmic surfaces of distinct membrane bound organelles. RAB14 has a role in vesicular trafficking and neurotransmitter release throughout the body and is expressed at high levels in brain, lung, kidney, spleen and thymus. In addition, RAB14 takes part in the biosynthetic/recycling pathway between the Golgi and endosomal compartments.

Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

RASD Family Member 2 (RASD2) which binds to GTP and owns a GTPase activity is a part of the Ras super family of small GTPases. RASD2 regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins. RASD2 encodes a Ras-related protein that enriched in striatum.

Guanine Nucleotide Binding Protein Gamma 12, also known as GNG12 belongs to the Guanine nucleotide-binding proteins (G proteins) which are involved as a modulator or transducer in a variety of transmembrane signaling systems. In addition, the beta as well as gamma chains are essential for the GTPase activity, for replacement of GDP by GTP, and also for G protein-effector interaction.

RHEB is part of the Ras & GTPase superfamily that was originally identified as an immediate-early gene in brain but is also widely expressed in other tissues. RHEB encodes a lipid-anchored, cell membrane protein with five repeats of the RAS-related GTP-binding region. RHEB is necessary in regulation of growth and cell cycle progression due to its role in the TOR/S6K signaling pathway. RHEB has GTPase activity and shuttles between a GDP-bound form and a GTP-bound form, and farnesylation of the protein is required for this activity. RHEB induces oncogenic transformation. RHEB overexpression accelerates lymphomagenesis and is associated with prostate cancer. RHEB can cytopathologically distinguish between fibroadenoma from malignant breast carcinomas which is considered as a secondary diagnostic tool. RHEB has a central role in the regulation of the Ras/B-Raf/C-Raf/MEK signaling network.

RAP1A is part of the family of RAS-related proteins which possess 50% amino acid identity with the classical RAS proteins and have various structural characteristics in common. RAP proteins differ from RAS proteins in their 61st amino acid, glutamine in RAS is replaced by threonine in RAP proteins. RAP1A induces morphological reversion of a cell line transformed by a Ras oncogene and counteracts the mitogenic function of Ras, since it can interact with Ras GAPs and RAF in a competitive manner.

RAN is a GTP-binding protein that participates in nucleocytoplasmic transport. RAN is necessary for the import of protein into the nucleus and also for RNA export. RAN takes part in chromatin condensation and control of cell cycle. The RAN complex with BIRC5 participates in mitotic spindle formation by being as a physical scaffold to assist the delivery of the RAN effector molecule TPX2 to microtubules. RUN increases AR-mediated transactivation.