PRKAR1A

cAMP-Dependent Protein Kinase A regulatory subunit I a Recombinant

Cat. No.

BT8468

Source

Escherichia Coli.

Synonyms

cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.

Appearance

Purity

Greater than 90% as determined by SDS-PAGE.

Usage

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

cAMP-dependent PKA is an ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant PKA regulatory subunit I a is a dimeric 90kDa protein.

Product Specs

Description

cAMP-dependent PKA is a serine/threonine protein kinase found in various tissues, including the brain, skeletal muscle, and heart. cAMP regulates cellular responses by influencing the interaction between PKA's catalytic (C) and regulatory (R) subunits. The inactive PKA holoenzyme (R2C2) is activated when cAMP binds to R2, causing the tetramer to dissociate into R2 cAMP 4 and two active catalytic subunits. These free catalytic subunits can then phosphorylate a range of intracellular target proteins. In response to hormone-induced elevated cAMP levels, PKA phosphorylates glycogen synthase and phosphorylase kinase, inhibiting glycogen synthesis. The existence of different isoforms of catalytic and regulatory subunits suggests specific functions for each. The recombinant PKA regulatory subunit I a is a dimeric protein with a molecular weight of 90kDa.

Formulation

PKA regulatory subunit I a is supplied in a 50% glycerol solution.

Stability

For use within 2-4 weeks, store at 4°C. For longer storage, freeze at -20°C. Avoid repeated freeze-thaw cycles.

Unit Definition

This product specifically inhibits PKA catalytic subunit with a Ki of approximately 0.1nM. Activity can be restored by adding cAMP (Kact approximately 100nM). The catalytic subunit's binding is dependent on the presence of ATP and Mg.

Purity

Purity is greater than 90% as determined by SDS-PAGE analysis.

Synonyms

cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.

Source

Escherichia Coli.

Product Science Overview

Introduction

cAMP-Dependent Protein Kinase A (PKA) is a crucial enzyme in cellular signaling, playing a significant role in various physiological processes. The regulatory subunit Iα (RIα) of PKA is particularly important for its function. Recombinant forms of this subunit are used extensively in research to study the enzyme’s mechanisms and interactions.

Structure and Function

PKA is a serine/threonine kinase that is activated by cyclic adenosine monophosphate (cAMP). It exists as a tetrameric holoenzyme composed of two regulatory ® subunits and two catalytic © subunits. The regulatory subunits inhibit the catalytic subunits in the absence of cAMP. Upon binding cAMP, the regulatory subunits undergo a conformational change that releases the catalytic subunits, allowing them to phosphorylate target proteins.

There are two major types of regulatory subunits: RI and RII. The RIα subunit is one of the isoforms of the RI type. It is encoded by the PRKAR1A gene and is primarily found in the cytosol. The RIα subunit has several domains, including a cAMP-binding domain, a domain that interacts with the catalytic subunit, and an auto-inhibitory domain.

Biological Significance

The balance between the different isoforms of PKA, including RIα, is crucial for cellular function. The RIα subunit is involved in regulating cell growth, proliferation, and differentiation. Mutations in the PRKAR1A gene, which encodes the RIα subunit, have been linked to Carney Complex, a condition characterized by an increased risk of benign and malignant tumors.

Recombinant RIα Subunit

Recombinant forms of the RIα subunit are produced using various expression systems, such as bacteria, yeast, and mammalian cells. These recombinant proteins are used in research to study the structure and function of PKA, as well as its interactions with other proteins and small molecules. Recombinant RIα subunits are also used in drug discovery to screen for compounds that can modulate PKA activity.

Applications in Research

Structural Studies: Recombinant RIα subunits are used to determine the three-dimensional structure of PKA and its complexes with other proteins and ligands.
Functional Assays: These subunits are used in biochemical assays to study the enzyme’s activity and regulation.
Drug Discovery: Recombinant RIα subunits are used in high-throughput screening assays to identify potential therapeutic agents that target PKA.

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PRKAR1A

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