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6-Chloroguanine riboside


  • Brand : BIOFRON

  • Catalogue Number : BN-O1057

  • Specification : 95%(HPLC)

  • CAS number : 2004-07-1

  • Formula : C10H12ClN5O4

  • Molecular Weight : 301.69

  • Volume : 5mg

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Catalogue Number


Analysis Method





Molecular Weight



Botanical Source

Structure Type





(−)-2-Amino-6-chloropurine riboside 6-Chloroguanine riboside/6-Chloroguanineriboside/2-Amino-6-chloro-9-(β-D-ribofuranosyl)purine/6-Chloro-9-(β-D-ribofuranosyl)-9H-purin-2-amine/(−)-2-Amino-6-chloropurine riboside/6-CHLOROGUANOSINE/2-Amino-6-chloropurine Riboside/6-Chloroguanine nucleoside/6-CHLOROADENOSINE/6-Chloroguanosine2/2-Amino-6-chloropurine-9--D-riboside/9H-Purin-2-amine, 6-chloro-9-β-D-ribofuranosyl-/6-Chloroguanine riboside/2-amino-6-chloro purineriboside



2.2±0.1 g/cm3


Flash Point

395.2±35.7 °C

Boiling Point

729.9±70.0 °C at 760 mmHg

Melting Point

165-167 °C (dec.)(lit.)


InChl Key

WGK Germany


HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:2004-07-1) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.




Under no-strand bias conditions, each genomic DNA strand should present equimolarities of A and T and of G and C. Deviations from these rules are attributed to asymmetric properties intrinsic to DNA mutation-repair processes. In bacteria, strand biases are associated with replication or transcription. In eukaryotes, recent studies demonstrate that human genes present transcription-coupled biases that might reflect transcription-coupled repair processes. Here, we study strand asymmetries in intron sequences of evolutionarily distant eukaryotes, and show that two superimposed intron biases can be distinguished. (i) Biases that are maximum at intron extremities and decrease over large distances to zero values in internal regions, possibly reflecting interactions between pre-mRNA and splicing machinery; these extend over ∼0.5 kb in mammals and Arabidopsis thaliana, and over 1 kb in Caenorhabditis elegans and Drosophila melanogaster. (ii) Biases that are constant along introns, possibly associated with transcription. Strikingly, in C.elegans, these latter biases extend over intergenic regions that separate co-oriented genes. When appropriately examined, all genomes present transcription-coupled excess of T over A in the coding strand. On the opposite, GC skews are either positive (mammals, plants) or negative (invertebrates). These results suggest that transcription-coupled asymmetries result from mutation-repair mechanisms that differ between vertebrates and invertebrates.


Transcription-coupled and splicing-coupled strand asymmetries in eukaryotic genomes


Marie Touchon, Alain Arneodo,1 Yves d'Aubenton-Carafa, and Claude Thermes*

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The yeast Snf1 protein kinase and its animal homologue, the AMP-activated protein kinase, play important roles in metabolic regulation, by serving as energy gauges that turn off energy-consuming processes and mobilize energy reserves during low-energy conditions. The closest homologue of these kinases in plants is Snf1-related protein kinase 1 (SnRK1). We have cloned two SnRK1-encoding genes, PpSNF1a and PpSNF1b, in the moss Physcomitrella patens, where gene function can be studied directly by gene targeting in the haploid gametophyte. A snf1a snf1b double knockout mutant is viable, but lacks all Snf1-like protein kinase activity. The mutant has a complex phenotype that includes developmental abnormalities, premature senescence and altered sensitivities to plant hormones. Remarkably, the double knockout mutant also requires continuous light, and is unable to grow in a normal day-night light cycle. This suggests that SnRK1 is needed for metabolic changes that help the plant cope with the dark hours of the night.


AMPK, metabolic regulation, Physcomitrella , Snf1, SnRK1


Snf1-related protein kinase 1 is needed for growth in a normal day-night light cycle


Mattias Thelander,1 Tina Olsson,1 and Hans Ronne1,a

Publish date

2004 Apr 21;




cENS-1/cERNI genes have been shown to be expressed very early during chicken embryonic development and as well as in pluripotent chicken embryonic stem (CES) cells. We have previously identified a promoter region, which is specifically active in CES cells compared to differentiated cells. In order to understand the molecular mechanisms which regulate the cENS-1/cERNI promoter, we analyzed the cis-acting elements of this promoter in CES and differentiated cells. We identified a short sequence, named the B region, 5′-CAAG TCCAGG CAAG-3′, that exhibits a strong enhancer activity in CES and differentiated cells. Mutation of the B region in the whole cENS-1 promoter strongly decreases the promoter activity in CES cells, suggesting that this region is essential for activating the promoter. The B region is similar to the previously described response element for the transcription factor CP2 and we show by supershift experiments that a protein complex containing CP2 is bound to this B response element. All these results identify a nuclear factor belonging to the CP2 transcription factor family that is crucial for the activation of the cENS-1/cERNI promoter. The pattern of expression of cCP2 in early chicken embryo before gastrulation is very similar to that of cENS-1/cERNI which strongly suggests that cCP2 also plays an essential role in gene expression early in embryonic development.


Transcription factor cCP2 controls gene expression in chicken embryonic stem cells


Herve Acloque,a Anne Mey, Anne Marie Birot, Henri Gruffat,1 Bertrand Pain, and Jacques Samarut*

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