P5015
Protein Kinase Inhibitor from rabbit muscle
lyophilized powder, 0.2-1 inhibitor U/μg protein
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About This Item
MDL number:
UNSPSC Code:
12352202
biological source
rabbit muscle
form
lyophilized powder
specific activity
0.2-1 inhibitor U/μg protein
composition
Protein, ~95% biuret
storage temp.
2-8°C
Biochem/physiol Actions
Binds to the catalytic subunit of cyclic-AMP dependent protein kinase, displacing the regulatory subunit and inhibiting phosphorylating activity. The cAMP binding capacity of the regulatory subunit is enhanced. The amino acid sequence deduced from cDNA is 100% homologous with human PKI.
Packaging
Package size based on protein content.
Physical form
Lyophilized powder containing 5% potassium phosphate buffer salts
Preparation Note
Fractionated essentially by procedure of Walsh, D.A., et al., J. Biol. Chem., 246, 1977 (1971), through TCA precipitation.
Analysis Note
Crude
Other Notes
One unit will transfer 1.0 picomole (10-12 mol) of phosphate from γ-32P-ATP to hydrolyzed and partially dephosphorylated casein (Product No. C 4765) per min at pH 6.5 at 30 °C.
Storage Class Code
13 - Non 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
Regulatory Information
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J Stern et al.
The Journal of general physiology, 85(2), 157-169 (1985-02-01)
The effect of intracellular nucleotides on the rate of spontaneous quantum bumps in Limulus ventral photoreceptors has been examined. Internal dialysis of photoreceptors with solutions lacking nucleotide leads to an elevation of the quantum bump rate that can be reversed
Protein phosphorylation and hydrogen ions modulate calcium-induced closure of gap junction channels.
R O Arellano et al.
Biophysical journal, 57(2), 363-367 (1990-02-01)
The regulation of the cell-to-cell pathway formed by gap junctions seems to involve the interaction of the junctional channels with either calcium or hydrogen ions, as well as protein phosphorylation and calmodulin. These mechanisms of junctional regulation have been considered
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