cAMP ELISA Kit

Sample

Urine, plasma, culture medium samples, cell samples, tissue samples

Species Reactivity

Universal

Detection Method

cELISA

Intended Use

This kit uses a competitive ELISA method to measure cAMP levels in cell extracts or in vitro adenylate cyclase assays.

Contents of Kit

Storage

cAMP Standard, cAMP-HRP Conjugate (1000×), cAMP monoclonal antibody (1000×): -20°C~-80°C
Other Reagents: 2-8°C

General Description

Cyclic adenosine monophosphate (cAMP) is an intracellular second messenger that is derived from the conversion of adenosine triphosphate catalysed by adenylyl cyclase (AC). Protein kinase A (PKA), the main effector of cAMP, is a dimeric protein kinase consisting of two catalytic subunits and two regulatory subunits. When cAMP binds to the regulatory subunits of PKA, it leads to the dissociation and activation of PKA, which allows the catalytic subunit of PKA to phosphorylate target proteins, thereby regulating various physiological functions and metabolic processes in cellular function. cAMP's notable characteristic lies in its ability to tightly regulate a wide range of physiological processes, including metabolism, homeostasis, secretion, muscle contraction, cell proliferation and migration, immune response, and gene transcription. The intracellular cAMP levels are regulated by cyclic nucleotide phosphodiesterases (PDEs). It is recognized that the action of phosphodiesterases is essential for the spatiotemporal regulation of cAMP levels. Research suggests that inhibitors of cAMP-specific phosphodiesterases can be used to treat human diseases.
People have been looking for a method to quickly, sensitively, specifically and reproducibly detect the content of cAMP. This can help people quickly understand the regulatory role of cAMP in various physiological processes. And it will be applied to related drug development and drug screening.

Standard Curve

General Notes

Cyclic adenosine monophosphate (cAMP) is an intracellular second messenger that is derived from the conversion of adenosine triphosphate catalysed by adenylyl cyclase (AC). Protein kinase A (PKA), the main effector of cAMP, is a dimeric protein kinase consisting of two catalytic subunits and two regulatory subunits. When cAMP binds to the regulatory subunits of PKA, it leads to the dissociation and activation of PKA, which allows the catalytic subunit of PKA to phosphorylate target proteins, thereby regulating various physiological functions and metabolic processes in cellular function. cAMP's notable characteristic lies in its ability to tightly regulate a wide range of physiological processes, including metabolism, homeostasis, secretion, muscle contraction, cell proliferation and migration, immune response, and gene transcription. The intracellular cAMP levels are regulated by cyclic nucleotide phosphodiesterases (PDEs). It is recognized that the action of phosphodiesterases is essential for the spatiotemporal regulation of cAMP levels. Research suggests that inhibitors of cAMP-specific phosphodiesterases can be used to treat human diseases.
People have been looking for a method to quickly, sensitively, specifically and reproducibly detect the content of cAMP. This can help people quickly understand the regulatory role of cAMP in various physiological processes. And it will be applied to related drug development and drug screening.