Tris/Glycine pH 7.4-7.9, 30%glycerol, BSA, and 0.02% sodium azide
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
0.5 mg/ml (Please refer to the vial label for the specific concentration.)
generated against peptide C-GTPTRKI(S92)ASEFDR containing PKG phosphorylation site and is conserved in many species.
Affinity purified with antigen
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
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 hydrolyze cGMP in various tissues is phosphodiesterase type 5A. Cyclic GMP is involved in nitric oxide signaling as well as cell signaling associated with natriuretic peptides and gulanylins. Some of the intracellular biding cites for the cGMP include cyclic nucleotide gated ion channels, cGMP-dependent protein kinases, and cyclic GMP biding phosphodiesterases (cGB-PDEs). The cGMP-PDEs include PDE2, PDE3, PDE5 and PDE9; the members of these families contain various structural and functional motifs that are conserved. Most of these proteins contain dimeric subunits that contain a highly conserved cGMP binding site and a phosphodiesterase catalytic site. The cGMP-specific phosphodiesterase type-5A (PDE5A) family is comprised of 2 genes (PDE5A and PDE5B) each with multiple splice variants generated by RNA splicing and use of alternate initiation sites. The PDE5 is highly expressed in aorta and lungs, intestine, kidney adrenal gland cerebellum and cerebrum. In cerebellum the PDE5 is highly expressed during neonatal development in Purkinge cells layer. The PDE5 is also abundant in vascular smooth muscle regulating cGMP levels and vascular smooth muscle tonicity in response to hormonal or mechanical stimulation . In corpus cavernosum inhibition of PDE5 by sildenafil corrects erectile dysfunctions. The nitric oxide donor sodium notropurside (SNP) stimulate PDE5 activity by cGMP-dependent kinase phosphorylation. The mechanism of PDE5A activity regulation in tissue is not fully understood, it is believed that phosphorylation of Ser92 affect this process. The serine 92 phosphorylation site is conserved in bovine, rat, humans, canine etc. The PDE5A can be phosphorylated in vitro by PKG or PKA. The amino terminal 142 amino acid of the PDE5 gene showed no sequence homology with other PDEs and also contained serine 92 that is phosphorylated by cGMP-kinases (McAllister et al., 93).