A 20aa Peptide sequence near C-terminus of Human CNG1.
The cyclic nucleotides cAMP and cGMP are implicated in signal transduction events such as the visual transduction, relaxation of smooth muscles, intestinal secretion of water and salt, reabsorption of Na+ and water in the distal tubule of the nephrons. cAMP/cGMP activate Ca2+ -permeable ion channels called cyclic nucleotide-gated channels (CNG or CNC). Activation of CNG leads to depolarization of the membrane voltage and to a concomitant increase of the cytosolic Ca2+. CNG consists of two distinct subunits, designated a and b subunits. Several CNG a-subunits (CNG alpha 1-3) & beta subunits (subunit 2 or CNGb1-2 or CNG4-5) and numerous isoforms. a-subunit can form functional channel by themselves, whereas, b-subunits modulate the channel property of a-subunits. CNG display intracellular N and C-termini, 6 transmembrane domains or segments (S1-S6). The region between S5 and S6 contains the ion-conducting pore (P). The cyclic nucleotide-binding region is found at the c-terminus. Native functional CNG may exists as heteromultimer containing some combination of a, and b subunits.
Bovine CNG1 was initially cloned and characterized from rod cells. CNG1 (rat 683 aa, mouse 684, human 686 aa; also describes as OCNC1) is primarily expressed in outer segment of photoreceptor rod cells, and in a variety of tissues (kidney, eye, pineal gland, pituitary, adrenal, spleen, brain, heart, skeletal muscle, and testis). Human/mouse CNG1 exhibit ~88% sequence homology.
仕様
Size：100ug
Source Antigen：Human synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide
Specificity：100% conserved in porcine, 80% in bovine, 70% in canine and 57% in rat (1-2). No significant sequence homology is detected with other CNGs. The control peptide, because of small size (MW 1.697kD), is not suitable for Western. It should be used for ELISA and antibody blocking to confirm specificity of antibodies
