A0144
Adenosine 3′,5′-cyclic monophosphate–Agarose
lyophilized powder
Synonym(s):
3′,5′-cAMP agarose
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About This Item
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form
lyophilized powder
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 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)
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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
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
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)
Purification of the cAMP receptor protein by affinity chromatography.
J Ramseyer et al.
Biochemical and biophysical research communications, 59(2), 813-821 (1974-07-24)
Adam J Funk et al.
Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 37(4), 896-905 (2011-11-04)
Recent evidence suggests that schizophrenia may result from alterations of integration of signaling mediated by multiple neurotransmitter systems. Abnormalities of associated intracellular signaling pathways may contribute to the pathophysiology of schizophrenia. Proteins and phospho-proteins comprising mitogen activated protein kinase (MAPK)
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