NewEast Biosciences pioneered the research and development of the antibodies for GTPases and mutated Oncogene ten years ago. GTPases involve (1) signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision, (2) protein biosynthesis at the ribosome, (3) regulation of cell differentiation, proliferation, division and movement, (4) translocation of proteins through membranes, (5) transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. An oncogene is a gene that has the potential to cause cancer.
We offer three unique categories of antibodies, which (1) recognize only the active configuration of GTPase (not the inactive one), (2) mutated Oncogene (not mild type) and (3) have super affinity for cAMP and cGMP (no acetylation required). We have over one thousand peer reviewed articles cited our products.
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GTPases are generally thought to be active when bound to GTP and inactive when bound to GDP, cycling between these two states regulated by two opposing protein families: guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). These are essential in dissociating tightly bound GDP from GTPases and promoting hydrolysis of GTP, respectively. Our Mouse Monoclonal Antibodies for GTP-bound G Proteins only recognize the active GTP-bound configuration, not inactive GDP-bound state. They have been used to monitor the activation of G protein in cells and in tissues by immunohistochemistry. The RAS superfamily of small GTPases. The 153 members of the RAS superfamily have been classified into five families based on sequence identify and cellular functions (Wennerberg et al. 2005; Wittinghofer and Vetter 2011). Representative members of each family and the main cellular functions are shown. |