PKAR-I alpha Human
Description
Product Specs
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE
EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQG
ETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V
Product Science Overview
Protein Kinase A (PKA) is a crucial enzyme in cellular signaling pathways, playing a significant role in regulating various physiological processes. The regulatory subunit-1 alpha (RIα) of PKA, encoded by the PRKAR1A gene, is essential for the proper functioning of this enzyme. This article delves into the background, structure, function, and clinical significance of the human recombinant form of PKA regulatory subunit-1 alpha.
PKA is a holoenzyme composed of two regulatory subunits and two catalytic subunits. The regulatory subunits control the activity of the catalytic subunits by binding to them and keeping them inactive. The RIα subunit, specifically, is one of the regulatory subunits that play a pivotal role in this regulation .
The PRKAR1A gene provides instructions for making the RIα subunit. When cyclic AMP (cAMP) levels rise in the cell, cAMP binds to the RIα subunits, causing a conformational change that releases the catalytic subunits. These free catalytic subunits then phosphorylate various target proteins, leading to a cascade of cellular responses .
Mutations in the PRKAR1A gene can lead to several disorders. One of the most notable conditions associated with PRKAR1A mutations is Carney Complex (CNC), a multiple neoplasia syndrome characterized by abnormal skin pigmentation, myxomas, and endocrine tumors . Additionally, inactivating mutations in PRKAR1A can cause primary pigmented nodular adrenocortical disease (PPNAD), which is associated with Cushing’s syndrome .
Research has shown that the depletion of RIα in mammalian cells activates the mechanistic target of rapamycin (mTOR) pathway, leading to autophagic deficiency . This finding has significant implications for understanding the molecular basis of diseases associated with autophagic deficiency, such as certain cancers and neurodegenerative disorders.
The human recombinant form of RIα is used in various research applications to study its role in cellular signaling and disease mechanisms. By using recombinant proteins, researchers can investigate the specific functions and interactions of RIα in a controlled environment, leading to a better understanding of its role in health and disease.
