PDE7A antibody

Background of PDE7A antibody

The cyclic monophosphate nucleotides (cyclic adenosine monophosphate [cAMP] and cyclic guanosine monophosphate [cGMP]) are found ubiquitously in mammalian cells and act as second messenger transducers to effect the intracellular actions of a variety of G-protein coupled receptors (GPCRs) for hormones, cytokines, and neurotransmitters. Cyclic nucleotides are important intracellular second messengers which play important role in a variety of signal transduction process. The cyclic nucleotides are hydrolyzed and compartmentalized by a family of enzymes called phosphodieterases. One of the many phosphodiesterases that compartmentalized and hydrolyze cAMP in T-Lymphocytes are phosphodiesterase type 7. The cAMP-specific phosphodiesterase type-7 (PDE7) family is comprised of 2 genes (PDE7A and PDE7B) each with multiple splice variants generated by RNA splicing and use of alternate initiation sites (1). PDE7A has two splice variants (PDE7A1 and PDE7A2), the two are divergent at the 5’ end in human and PDE7A1 is more hydrophobic (2). Like other PDEs, human PDE7A gene has 456 amino acids and migrates at an apparent molecular weight of 53-55 kDa on reduced SDS-PAGE. The PDE7A has a significant conserved region of about 270 amino acids common to all PDEs at the carboxy terminal apparently serves as the catalytic domain. The amino-terminal region of this protein is divergent and presumably accounts for the distinctive and regulatory properties unique to the individual PDE families. PDE7A protein showed significant homology to other cAMP-dependent PDEs (23%) with in the catalytic domain. PDE7A is widely expressed in various tissues including skeletal muscle, T lymphocytes, brain, pancreas,