產品名稱：cAMP RIA DAb
產    地：Demeditec 
產品貨號：DEBT300
產品規格：200 Tests
其它產品：
cGMP Demeditec DEBT340 200 Tests 7370
產品說明：
Special remarks: Cyclic AMP was discovered by Sutherland and others in the 1950's.  It has since been well established that cAMP mediates the cellular action of numerous hormones in virtually all animals, plants and bacteria. Generally, this interaction occurs at the plasma membrane where the hormone binds the cell and activates the cAMP generating enzyme, adenyl cyclase. The resulting increases in intracellular cAMP modifies a variety of biological responses.
cAMP is synthesised from ATP by adenylate cyclase which is located at the cell membranes. Adenylate cyclase is activated by the hormones glucagon and epinepherine through the activation of adenylate cyclase stimulatory G (Gs)-coupled receptors and inhibited by agonists of adenylate cyclase inhibitory G (Gi)-protein coupled receptors. Liver adenylate cyclase responds more strongly to glucagon, and muscle adenylate cyclase responds more strongly to adrenaline.
cAMP decomposition into AMP is catalyzed by the enzyme phosphodiesterase.
Cyclic AMP is involved in some protein kinases. For example, PKA (protein kinase A, also known as cAMP-dependent protein kinase) is normally inactive as a tetrameric holoenzyme, consisting of 2 catalytic and 2 regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units.
cAMP controls many biological processes, including glycogen decomposition into glucose (glycogenolysis), and lipolysis. Glycogen phosphorylase is the enzyme used to produce glucose from glycogen when the sugar is required in muscle tissue. However, the enzyme is present all the time in its inactive, non-phosphorylated form. cAMP is required to activate the protein kinases required for the phosphorylation process. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins.
In bacteria, the level of cAMP varies depending on the medium used for growth. In particular, cAMP is low when glucose is the carbon source. This occurs through inhibition of the cAMP-producing enzyme, adenylate cyclase, as a side effect of glucose transport into the cell. The transcription factor CRP (cAMP receptor protein) also called: CAP (Catabolite gene Activator Protein) forms a complex with cAMP and thereby is activated to bind to DNA. CRP-cAMP increases expression of a large number of genes, including some encoding enzymes that can supply energy independent of glucose.
An example of cAMP's function is the positive regulation of the lac operon. In an environment of a low glucose concentration, cAMP accumulates and binds to the allosteric site on CRP, a transcription activator protein. The protein assumes its active shape and binds to a specific site beside the lac promoter, making it easier for RNA polymerase to bind to the adjacent promoter to start transcription of the lac operon, increasing the rate of lac operon transcription. With a high glucose concentration, the cAMP concentration decreases, and the CRP disengages from the lac operon.
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