A0144
Adenosine 3′,5′-cyclic monophosphate–Agarose
lyophilized powder
Synonym(s):
3′,5′-cAMP agarose
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1 ML
$124.00
5 ML
$421.00
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1 ML
$124.00
5 ML
$421.00
About This Item
$124.00
Check Cart for Availability
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form
lyophilized powder
Quality Level
extent of labeling
≥2 μmol per mL
matrix
4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
C-8
matrix spacer
9 atoms
storage temp.
−20°C
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Application
Adenosine 3′,5′-cyclic monophosphate-Agarose (3′,5′-cAMP agarose) may be used in affinity chromatography for the separation of the subunits of cAMP-dependent protein kinase or for the purification of the cAMP receptor subunit. Research on schizophrenia has shown that abnormalities in the cAMP signaling pathway, may contribute to the pathophysiology of the disorder.
Physical form
Lyophilized powder stabilized with lactose
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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R G Panchal et al.
The Journal of biological chemistry, 269(38), 23722-23730 (1994-09-23)
cAMP-dependent protein kinase (PKA) is an important participant in neuronal modulation: the ability of neurons to change their properties in response to external stimuli. In Aplysia mechanosensory neurons, PKA plays roles in both short and long term presynaptic facilitation, which
K Laukens et al.
FEBS letters, 508(1), 75-79 (2001-11-15)
The soluble protein fraction of tobacco bright yellow 2 cells contained adenosine 3',5'-cyclic monophosphate (cAMP)-binding activity, detected with both a conventional binding assay and a surface plasmon resonance biosensor. A cAMP-agarose-based affinity purification procedure yielded three proteins which were identified
Florencia Kronberg et al.
Archives of biochemistry and biophysics, 509(1), 66-75 (2011-03-09)
cAMP-dependent protein kinase (PKA) catalytic (C) and regulatory (R) subunits from Yarrowia lipolytica are encoded by single genes, TPK1 and RKA1, respectively. Here we performed the heterologous expression, purification and characterization of the R subunit from Y. lipolytica yeast cells
Purification of rabbit skeletal muscle protein kinase regulatory subunit using cyclic adenosine-3':5'-monophosphate affinity chromatography.
W L Dills et al.
Biochemical and biophysical research communications, 62(1), 70-77 (1975-01-06)
J P Huggins et al.
European journal of biochemistry, 221(1), 581-593 (1994-04-01)
The structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide (peptide-546) and its effects on cGMP-dependent protein kinase I alpha (G-kinase) have been studied. By primary sequence analysis and analogy to a peptide that stimulates protein kinase C, peptide-546 was predicted
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