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ULS Labelling
The proprietary ULS™ technology provides the basis of KREATECH's broad range of labelling-based applications for FISH, arrayCGH, miRNA microarrays, gene expression microarrays, protein arrays and others. ULS labelling is based on the stable binding properties of platinum(II) to nucleic acids and proteins. The ULS molecule consists of a monofunctional platinum complex coupled to a detectable molecule of choice. The platinum atom forms a coordinative bond, firmly coupling the detectable molecule to the biomolecule of choice: DNA, RNA or protein. ULS labels DNA and RNA by binding to N-7 of guanine. In proteins, ULS binds to sulfur-containing side chains of methionine, and cysteine, and to a nitrogen atom in histidine (see figures below). |



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General:
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Chemical labelling method (no enzymes required)
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Easy to control reaction conditions resulting in optimal control over the degree of labelling which is reproducible
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Easily scalable to the amount of sample to be labeled
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Stable in aqueous solutions (enabling automation) and stored at 4°C
Nucleic acid labelling
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Uniform labelling of native DNA, RNA and oligonucleotides as well as enzymatically amplified nucleic acids (e.g. PCR, WGA, aRNA products)
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Size independent labelling of nucleic acids; e.g. ranging from miRNA (20mer) to genomic DNA (>20kb)
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Suitable for the labelling of 3' / 5' modified nucleic acids (e.g. plant and germ-line miRNA)
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Suitable for the labelling of native bacterial mRNA
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Efficiently labels nucleic acids from archival material such as DNA/RNA isolated from formalin-fixed paraffin-embedded (FFPE) tissue
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Optimal removal of unreacted label using KREApure™ columns
Protein labelling
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Labels methionine, cysteine and histidine containing proteins and peptides
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High coverage of the proteome (>98%) required for labelling complex protein mixtures
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Labels proteins from any type of sample, like cell lysate, plasma, serum, and even proteins extracted from formalin-fixed paraffin-embedded (FFPE) tissue
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Low chance of interference with epitope recognition or protein interaction domains
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Optimal removal of unreacted label using ULS-Trap™ columns
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Labels independent of pH and is compatible with many salts and buffers including Tris and glycine
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