cAMP

cAMP-dependent protein kinase (PKA) is a Ser/Thr protein kinase that is highly conserved between species. Three distinct catalytic (C) subunits have been identified, designated C-alpha, C-beta and C-gamma, where C-alpha and C-beta are most closely related. PKA mediates a variety of diverse cellular responses (cell growth and proliferation, ion transport, triglyceride storage and metabolism regulation, embryonic development, and gene transcription) in virtually all eukaryotic systems via phosphorylation of a wide range of downstream target proteins in both they cytoplasm and nucleus.

The CXCR4 (C-X-C chemokine receptor type 4) protein is one member of the G-protein coupled receptor (GPCR1) family. As a multipass membrane protein that is found in several tissues, it is the receptor for the C-X-C chemokine CXCL12/SDF-1. The CXCR4 ligand works by modulating intracellular calcium ion levels and activating the MAPK1/MAPK3 signal pathways. CXCR4 is also a receptor for extracellular ubiquitin, which produces enhanced levels of intracellular calcium and reduced levels of cellular cAMP.

A-kinase anchor proteins (AKAPs), such as AKAP95/AKAP8, are scaffold proteins that contain a binding domain for the RI/RII subunit of protein kinase A (PKA). AKAPs orchestrate and synchronize cellular events by tethering the cAMP-dependent PKA and other signaling enzymes to organelles and membranes. This gene encodes a nuclear A-kinase anchor protein that binds to the RII alpha subunit of PKA and may play a role in chromosome condensation during mitosis (1).

The G-protein coupled receptor (GPCR) family constitutes one of the largest protein families in the mammalian kingdom, with over 800 proteins so far discovered. Our GPCR antibody catalog covers all 6 classes, with antibodies raised against Metabotropic Glutamate/Pheromone receptors; Rhodopsin-like receptors; Secretin receptors; Fungal Mating Pheromone receptors; cAMP receptors and Frizzled/Smoothened receptors. The majority are of the Class A (Rhodopsin-like) class.