Skip to Content
Merck
All Photos(1)

Documents

P5511

Sigma-Aldrich

Protein Kinase A from bovine heart

≥0.8 units/μg protein, lyophilized powder

Synonym(s):

Protein Kinase, 3′,5′-cyclic-AMP-dependent from bovine heart

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.77

form

lyophilized powder

specific activity

≥0.8 units/μg protein

composition

Protein, ≥70%

UniProt accession no.

storage temp.

−20°C

Gene Information

Looking for similar products? Visit Product Comparison Guide

General description

Protein Kinase A (PKA) is a serine/threonine kinase, which exists as a tetrameric holoenzyme.

Application

Protein Kinase A from bovine heart has been used to determine its activity using a molecular beacon probe. It has also been used to study the interaction of staurosporine with the ATP-binding site of kinases.
Protein Kinase A from bovine heart has been used to inhibit the phosphorylation of myosin.

Biochem/physiol Actions

Protein Kinase A (PKA) inhibits hormone-sensitive lipase translocation from cytosol to storage droplets and blocks lipolysis. It regulates apoptosis, mitochondrial respiration and ATP synthesis. PKA is modulated by protease calpain.
Many 3′,5′-cyclic AMP dependent protein kinases have been reported. Structural studies (Traugh, J.A., et al., Meth. Enzymol., 38, 290 [1974]) show the presence of at least two subunits, the regulatory subunit and the catalytic subunit. When both units are linked together, the catalytic activity is inhibited. However, when the cyclic-AMP binds to the regulatory subunit, the catalytic subunit is released and can then catalyze the transfer of phosphate from ATP to various proteins.

Packaging

Package size based on protein content

Unit Definition

One unit will transfer 1.0 picomole phosphate from ATP to hydrolyzed and partially dephosphorylated casein per minute at pH 6.5 at 30°C in the presence of cyclic AMP, determined by measuring the production of ADP.

Physical form

Crude lyophilized powder containing EDTA and potassium phosphate, pH 7.5.

Preparation Note

Fractionated essentially by procedure of Gilman, A., Proc. Natl. Acad. Sci. USA, 67, 305 (1970).

Analysis Note

Protein determined by biuret.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Probes of the mitochondrial cAMP-dependent protein kinase
Shell JR and Lawrence DS
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1834(7), 1359-1363 (2013)
Nitroglycerine-and isoprenaline-induced vasodilatation: assessment from the actions of cyclic nucleotides
Itohy T, et al.
British Journal of Pharmacology, 84(2), 393-406 (1985)
Péter Enyedi et al.
PloS one, 9(5), e97854-e97854 (2014-05-17)
The cytoplasmic loop between the second and third transmembrane segments is pivotal in the regulation of TRESK (TWIK-related spinal cord K+ channel, K2P18.1, KCNK18). Calcineurin binds to this region and activates the channel by dephosphorylation in response to the calcium
Y Ito et al.
British journal of pharmacology, 83(3), 677-686 (1984-11-01)
Effects of isoprenaline (Isop) on the contractile properties of the smooth muscle cells of cat trachea were investigated using intact and chemically skinned muscle preparations and an isometric tension recording method. In the intact muscle preparations, Isop 3 X 10(-10)
Alkylation of Staurosporine to Derive a Kinase Probe for Fluorescence Applications
Dr. Alexandar
Chemistry of Materials (2016)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service