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Integrated DNA
Technologies, BVBA
Provisorium 2
Minderbroedersstraat 17-19
B-3000 Leuven
BELGIUM
Tel: +32-16-337096
Fax: +32-16-337097
info@rna-tec.com
How to reach us
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Intermediate scale
oligonucleotides
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Scale: Synthesis scales range from 10
µmol to several mmol. This corresponds
with quantities of 10 mg to several grams.
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Purity: Our standard purity > 95%,
purities of 99 % as determined by analytical
HPLC are available on request.We have
completely optimized purification methods
customized for each oligo depending on its
length, its likeliness to form secondary
structures, the purity requirement and the
required counterion.
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Yield: Our expertise in the field of
nucleotide and nucleoside chemistry enables us
to perform oligonucleotide synthesis with the
highest yield in a cost effective format. For
more info click complexity and cost
efficiency.
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Standard RNA & DNA: In our
portfolio we have the above mentioned scales
of standard RNA and DNA oligos. RNA oligos up
to lengths of 45 bases are standard. For
longer RNA oligos, please inquire.
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Chimeras and modifications: Synthesis
of complex chimeras and aptamers containing
almost any commercially available monomer is
also offered.
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Delivery: All our products are fully
desalted and supplied as sodium salts in
lyophilized form. Of course other salts can be
supplied when required. Delivery is with FedEx
and is free of charge for orders > 1000
Euro.
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Quality control: Extensive quality
controls is supplied with all the data, free
of charge. For more info concerning our
quality control click quality
control.
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RNA - Peptide conjugates
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The cellular uptake of oligonucleotides in
vivo is a fundamental issue that has
challenged scientists in the antisense field
and is now a major issue for the in vivo /
therapeutic application of siRNA.
It has been demonstrated that a variety of
peptides enhance cellular uptake of
oligonucleotides when conjugated to them, thus
avoiding the usage of liposomes, many of which
are toxic in vivo.
RNA-TEC now offers custom synthesis of
RNA-peptide conjugates in which the linkage
between the oligo and the peptide is stable or
biodegradable.
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Custom synthesis
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Custom synthesis of various nucleotide related
complex molecules e.g. aminoacyl adenylate
analogues as inhibitors of aminoacyl t-RNA
synthetases. Various research programs are
supplied with complex molecules, but are
confidential.
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We are very pleased to offer
5´-O-[N-(L-aminoacyl)sulfamoyl]adenosines
for sale as stable analogues of aminoacyl
adenylates. These compounds have the general
structure shown below, where R represents an amino
acid side-chain, and are potent inhibitors of the
corresponding aminoacyl-tRNA synthetases. To date the alanyl (1-3), arginyl (4), asparaginyl (5, 24), aspartyl (13), cysteinyl (3), glutaminyl (6, 7), glutamyl (14), glycyl (1, 15), histidyl (4, 8), isoleucyl (21), lysyl (9), prolyl (3, 10, 16), seryl (11, 17), threonyl (4, 12, 18, 19), tyrosyl (20, 23) and valyl (22) analogues have been described in publications.
We envisage that these compounds should be of
general interest to all scientists working on
aminoacyl-tRNA synthetases.
Of course we would be very happy to custom
synthesize other analogues such as norvalyl, so
please contact us for a quotation.
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PRODUCT
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QUANTITY
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CODE
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PRICE(€)
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| Alanyl analogue
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10 mg
50 mg
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Ala-SA-10
Ala-SA-50
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250
1000
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| Arginyl analogue
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10 mg
50 mg
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Arg-SA-10
Arg-SA-50
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375
1500
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| Asparaginyl analogue
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10 mg
50 mg
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Asn-SA-10
Asn-SA-50
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313
1250
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| Aspartyl analogue
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10 mg
50 mg
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Asp-SA-10
Asp-SA-50
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250
1000
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| Cysteinyl analogue
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10 mg
50 mg
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Cys-SA-10
Cys-SA-50
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375
1500
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| Glutaminyl analogue
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10 mg
50 mg
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Gln-SA-10
Gln-SA-50
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800
3200
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| Glutamyl analogue
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10 mg
50 mg
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Glu-SA-10
Glu-SA-50
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250
1000
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| Glycyl analogue
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10 mg
50 mg
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Gly-SA-10
Gly-SA-50
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274
1100
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| Histidyl analogue
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10 mg
50 mg
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His-SA-10
His-SA-50
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375
1500
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| Isoleucyl analogue
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10 mg
50 mg
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Ile-SA-10
Ile-SA-50
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250
1000
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| Leucyl analogue
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10 mg
50 mg
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Leu-SA-10
Leu-SA-50
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250
1000
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| Lysyl analogue
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10 mg
50 mg
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Lys-SA-10
Lys-SA-50
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375
1500
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| Methionyl analogue
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10 mg
50 mg
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Met-SA-10
Met-SA-50
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375
1500
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| Phenylalanyl analogue
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10 mg
50 mg
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Phe-SA-10
Phe-SA-50
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250
1000
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| Prolyl analogue
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10 mg
50 mg
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Pro-SA-10
Pro-SA-10
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250
1000
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| Seryl analogue
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10 mg
50 mg
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Ser-SA-10
Ser-SA-50
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313
1250
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| Threonyl analogue
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10 mg
50 mg
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Thr-SA-10
Thr-SA-50
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313
1250
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| Tryptophanyl analogue
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10 mg
50 mg
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Trp-SA-10
Trp-SA-50
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800
3200
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| Tyrosyl analogue
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10 mg
50 mg
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Tyr-SA-10
Tyr-SA-50
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313
1250
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| Valyl analogue
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10 mg
50 mg
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Val-SA-10
Val-SA-50
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250
1000
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Larger quantities than those indicated are
available upon request.
All compounds have been purified by preparative
reversed phase HPLC and have a guaranteed purity of
greater than 97% as determined by analytical
reversed phase HPLC.
Each product is supplied in lyophilized form and is
delivered with a data and QC sheet plus a reversed
phase HPLC trace and a copy of the mass spectrum.
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- Castro-Pichel, J. et al. (1987). A facile synthesis of ascamycin and related analogues. Tetrahedron 43, 383-389.
- Ueda, H. et al. (1991). X-ray crystallographic conformational study of 5ยด-O-[N-(L-alanyl)-sulfamoyl]adenosine, a substrate analogue for alanyl-tRNA synthetase. Biochim. Biophys. Acta 1080, 126-134.
- Kamtekar, S. et al. (2003). The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. Proc. Natl. Acad. Sci. USA 100,
1673-1678.
- Forrest, A. K. et al. (2000). Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl tRNA synthetases. Bioorg. Med. Chem. Letters 10,
1871-1874.
- Berthet-Colominas, C. et al. (1998). The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid. EMBO J.
17, 2947-2960.
- Rath, V. L. et al. (1998). How glutaminyl-tRNA synthetase selects glutamine. Structure 6, 439-449.
- Sherlin, L. D. et al. (2000). Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases. J. Mol. Biol. 299, 431-446.
- Bovee, M. L. et al. (1999). tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase. Biochemistry 38, 13725-13735.
- Cusack, S. et al. (1996). The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed with E. coli tRNALys and a T. thermophilus tRNALys transcript: anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue. EMBO J. 15, 6321-6334.
- Heacock, D. et al. (1996). Synthesis and aminoacyl-tRNA synthetase inhibitory activity of prolyl adenylate analogs. Bioorg. Chem. 24, 273-289.
- Belrhali, H. et al. (1994). Crystal structures at 2.5 Angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate. Science
263, 1432-1436.
- Sankaranarayanan, R. et al. (2000). Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase. Nature Structural Biology 7, 461-465.
- Bernier, S. et al. (2005). Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogs. Bioorg. Med. Chem. 13,
69-75.
- Bernier, S. et al. (2005). Glutamylsulfamoyladenosine and pyroglutamylsulfamoyladenosine are copmpetitive inhibitors of E. coli glutamyl-tRNA synthetase. J. Enzyme Inhib. Med. Chem. 20, 61-67.
- Dignam, J.D. et al. (2003). Thermodynamic characterization of the binding of nucleotides to glycyl-tRNA synthetase. Biochemistry 42, 5333-5340.
- Bunjun, S. et al. (2000). A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia. Proc. Natl. Acad. Sci. USA 97,
12997-13002.
- Landeka, I. et al. (2000). Characterization of yeast seryl-tRNA synthetase active site mutants with improved discrimination against substrate analogues. Biochim. Biophys. Acta 1480, 160-170.
- Bovee, M.L. et al. (2003). Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. Biochemistry 42,
15102-15113.
- Fukunaga, R. & Yokoyama, S. (2005). Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain. J. Biol. Chem.
280, 29937-29945.
- Kotik-Kogan, O. et al. (2005). Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase. Structure 13,
1799-1807.
- Nakama, T. et al. (2001). Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J. Biol. Chem. 276,
47387-47393.
- Fukunaga, R. & Yokoyama, S. (2004). Crystallization and preliminary X-ray crystallography study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues. Acta Crystallogr. D Biol. Crystallogr. 60, 1900-1902.
- Kobayashi, T. et al. (2005). Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase. J. Mol. Biol.
346, 105-117.
- Iwasaki, W. et al. (2006). Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. J. Mol. Biol. 360,
329-342.
- Vaughan, M. et al. (2005). Investigation of bioisosteric effects on the interactionof substrates/inhibitors with the methionyl-tRNA synthetase from Escherichia coli. Med. Chem. 1, 227-237.
- Kanatani, K. et al. (2005). A simple approach to sense codon-templated synthesis of natural/unnatural hybrid peptides. Nucleic Acids Symp. Ser. 49, 265-266.
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