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Detail of "32115-08-5"

  • CAS Number:
  • 32115-08-5
  • Name:
  • Adenosine,N-(phenylmethyl)-, cyclic 3',5'-(hydrogen phosphate)

  • Molecular Structure:
  • Formula:
  • C17H18 N5 O6 P
  • Molecular Weight:
  • 419.3285
  • Synonyms:
  • Adenosine,N-benzyl-, cyclic 3',5'-(hydrogen phosphate) (8CI);4H-Furo[3,2-d]-1,3,2-dioxaphosphorin, adenosine deriv.; 6-(Benzylamino)purineriboside 3',5'-monophosphate; 6-Benzylamino-3',5'-purine riboside3',5'-monophosphate; Cyclic 6-benzylamino-3',5'-PuMP; N-Benzyladenosine cyclicmonophosphate; N6-Benzyl-9-b-D-ribofuranosyladenine cyclic 3',5'-monophosphate; N6-Benzyl-cAMP;N6-Benzyl-cyclic AMP; N6-Benzyladenosine 3',5'-cyclic phosphate;N6-Benzyladenosine 3',5'-monophosphate
  • Density:
  • 1.86 g/cm3
  • Boiling Point:
  • 719.8 °C at 760 mmHg
  • Flash Point:
  • 389.1 °C
  • Solubility:
  • at 25 deg C (mg/L): 250.6

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CAS No.32115-08-5 Adenosine,N-(phenylmethyl)-, cyclic 3',5'-(hydrogen phosphate)

Supplier:BIOLOG [ Germany]

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Reference

The use of cAMP analogs to study cAMP-dependent protein kinase-mediated events in intact mammalian cells
The use of cAMP analogs to study cAMP-dependent protein kinase-mediated events in intact mammalian cells. Beebe, S. J.; Blackmore, P. F.; Segaloff, D. L.; Koch, S. R.; Burks, D.; Limbird, L. E.; Granner, D. K.; Corbin, J. D. (Med. Cent., Vanderbilt Univ., Nashville, TN 37232, USA). Inst. Natl. Sante Rech. Med., [Colloq.], 139(Horm. Cell Regul.), 159-80 (English) 1986. CODEN: CINMDE. ISSN: 0768-3154. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Section cross-reference(s): 2 CAMP analogs were used in several intact mammalian cell prepns. to study physiol. responses mediated by the cAMP-dependent protein kinase (cA PK). These included adipocyte lipolysis, hepatocyte glycogenolysis, H4 hepatoma cell phosphoenolpyruvate carboxykinase gene transcription, and granulosa cell LH receptor induction and progesterone synthesis. The basic principles which detd. the efficacy of the analogs in stimulating these responses were: the partitioning characteristic of the analog, the concn. of analog required for protein kinase activation in vitro, and the susceptibility of the analogs to hydrolysis by phosphodiesterases. The efficacy of the analogs differed among the various cell types. For example, hepatocyte glycogenolysis was 100-10,000 times more sensitive to analog stimulation than was adipocyte lipolysis. To det. if cA PK was responsible for a cAMP effect, advantage was taken of a unique property of cA PK. The cA PK can be synergistically activated in vitro and in vivo by using pairs of cAMP analogs, each one selective for one or the other of 2 intrasubunit cAMP binding sites (Site 1 and Site 2) on cA PK. Various Site 1- and Site 2-selective analogs were added alone (in the linear dose-response range) and in combination, both in vitro to Type I and(or) Type II cA PK isolated from various cell types, and to intact cells. Correlations were then made between the extent of synergism of cA PK activation and the synergism of the various physiol. responses. All analog pairs which resulted in a synergistic activation of the resp. cA PKs resulted in a synergistic increase in all the resp. intact cell responses mentioned above. For all responses tested, synergism occurred only when Site 1- and Site 2-selective analogs were combined, a cA PK-specific characteristic. 31319-90-1 and 32115-08-5 are just another two chemicals used in this study. Because the synergism of cA PK, activation was strongly correlated with the synergism of the intact cell responses. CA PK could be entirely responsible for the cAMP activation of all the physiol. responses tested. .
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