Product List

PKACa2- RIa2

Inactive Protein Kinase A holoenzyme type I alpha Recombinant

Inactive holoenzyme consisting of one dimeric regulatory subunit type I alpha and two monomeric catalytic subunits (cAMP-free).
Protein Kinase A Recombinant is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8009
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PKACa2-RIIa2

Protein Kinase A holoenzyme type II alpha Recombinant

Inactive holoenzyme consisting of one dimeric regulatory subunit type II alpha and two monomeric catalytic subunits (cAMP-free).
Protein Kinase A is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8083
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PKAR-I alpha Human

Protein Kinase A regulatory subunit-1 alpha Human Recombinant

PKA regulatory subunit I a Human Recombinant is a dimeric 86kDa protein (the monomer is 381 aa 43kDa). PKAR-I alpha is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8179
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PKA-RII alpha

cAMP-Dependent Protein Kinase A regulatory subunit-II A Recombinant

The recombinant PKA regulatory subunit II-a is a dimeric 90 kDa protein.
Protein Kinase A is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8231
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PRKACA Human

cAMP-Dependent Protein Kinase A catalytic subunit α Human Recombinant

cAMP-dependent PKA is an ubiquitous serine/threonine 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 catalytic 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 catalytic subunit a is a 41kDa protein. The a-isoform is the predominant form with a broad tissue distribution and can be used for in vitro enzymological studies of neural and hormonal signal transduction or to phosphorylate target proteins in vivo including Ion channels, transcriptional activator proteins and regulatory enzymes of glycogen metabolism.
Shipped with Ice Packs
Cat. No.
BT8328
Source
Escherichia Coli.
Appearance

PRKACA Human, sf9

c-AMP dependant Protein Kinase A catalytic subunit alpha Human Recombinant, Sf9

PRKACA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (1-351 a.a.) and having a molecular mass of 67kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). PRKACA is expressed with a 227 amino acid GST Tag at N-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8401
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

PRKAR1A

cAMP-Dependent Protein Kinase A regulatory subunit I a Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT8468
Source
Escherichia Coli.
Appearance

Introduction

Definition and Classification

Protein Kinase-A (PKA), also known as cAMP-dependent protein kinase, is a family of serine-threonine kinases whose activity is dependent on cellular levels of cyclic AMP (cAMP) . PKA plays a crucial role in regulating various cellular processes, including metabolism, gene expression, and cell cycle progression . It is classified into two main types based on its regulatory subunits: Type I (PKA-I) and Type II (PKA-II) .

Biological Properties

Key Biological Properties: PKA is a tetrameric holoenzyme composed of two regulatory subunits and two catalytic subunits . The catalytic subunits contain the active site, while the regulatory subunits bind cAMP, leading to the activation of the catalytic subunits .

Expression Patterns and Tissue Distribution: PKA is ubiquitously expressed in various tissues, with different isoforms showing distinct expression patterns . Type I PKA is primarily found in the cytosol, whereas Type II PKA is associated with cellular membranes, including the plasma membrane, nuclear membrane, and mitochondrial outer membrane .

Biological Functions

Primary Biological Functions: PKA regulates a wide range of cellular functions, including glycogen, sugar, and lipid metabolism . It also plays a role in cell growth, proliferation, differentiation, and apoptosis .

Role in Immune Responses and Pathogen Recognition: PKA is involved in modulating immune responses by phosphorylating various immune-related proteins and transcription factors . It also plays a role in pathogen recognition and the activation of immune cells .

Modes of Action

Mechanisms with Other Molecules and Cells: PKA exerts its effects by phosphorylating specific serine and threonine residues on target proteins . This phosphorylation can activate or inhibit the function of the target proteins, leading to various cellular responses .

Binding Partners and Downstream Signaling Cascades: PKA interacts with multiple binding partners, including A-kinase anchoring proteins (AKAPs), which localize PKA to specific cellular compartments . Upon activation, PKA phosphorylates downstream effectors such as CREB (cAMP response element-binding protein), leading to changes in gene expression .

Regulatory Mechanisms

Control of Expression and Activity: The activity of PKA is primarily regulated by the intracellular concentration of cAMP . When cAMP levels are low, the catalytic subunits are bound to the regulatory subunits and are inactive . Upon binding of cAMP to the regulatory subunits, the catalytic subunits are released and become active .

Transcriptional Regulation and Post-Translational Modifications: PKA activity can also be modulated by transcriptional regulation of its subunits and post-translational modifications such as phosphorylation . These regulatory mechanisms ensure precise control of PKA activity in response to various cellular signals .

Applications

Biomedical Research: PKA is extensively studied in biomedical research due to its involvement in numerous cellular processes and diseases . It serves as a model for understanding kinase signaling and regulation .

Diagnostic Tools and Therapeutic Strategies: PKA activity and expression levels are used as biomarkers for certain diseases . Additionally, targeting PKA signaling pathways has therapeutic potential for treating conditions such as cancer, cardiovascular diseases, and metabolic disorders .

Role in the Life Cycle

Development to Aging and Disease: PKA plays a critical role throughout the life cycle, from development to aging . During development, PKA regulates cell differentiation and tissue formation . In adulthood, it maintains cellular homeostasis and responds to various physiological stimuli . Dysregulation of PKA activity is associated with aging and the development of age-related diseases .

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