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A0144

Sigma-Aldrich

Adenosine 3′,5′-cyclic monophosphate–Agarose

lyophilized powder

Sinónimos:

3′,5′-cAMP agarose

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About This Item

MDL number:
MFCD00161946
UNSPSC Code:
41106500
eCl@ss:
32160414
NACRES:
NA.56

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

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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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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