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Description:
Fibrous cellulose impregnated with polyethyleneimine available as POLYGRAM® polyester sheets with or without fluorescent indicator. They are used in analysis of nucleic acids and of mutagenic substances with the ³²P post labelling procedure.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3 UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3 UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.
Description:
RNA-Solv® Reagent est un système à un seul réactif pour isoler l'ARN total des cellules et des tissus. Le réactif, une solution monophasée constituée de phénol et d'isothiocyanate de guanidine, est une modification du procédé d'isolement de l'ARN en une seule étape développé par Chomczynski et Sacchi. L'échantillon est homogénéisé et lysé dans le réactif RNA-Solv® Reagent, qui maintient l'intégrité de l'ARN tout en interférant et dénaturant les RNases endogènes et autres composants cellulaires. L'extraction du lysat avec du chloroforme dénature davantage les protéines et divise le mélange en une phase organique et une phase aqueuse. L'ARN reste exclusivement dans la phase aqueuse, et est ensuite récupéré par isopropanol.
Description:
Digoxigenin-labeled nucleotide suitable for non-radioactive labeling of RNA probes.
UOM:
1 * 250 Nmo
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