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In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

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These trousers for women are a modern take on the traditional chino, offering a professional look without compromising comfort. The fabric is powered by Alsiflex technology, which provides a unique combination of stretch, sustainability and performance.

Supplier: Bioss

The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

Supplier: Bioss

ANKRD17 is a 2,603 amino acid protein that contains 25 ankyrin repeats and one KH domain. ANKRD17 is expressed in bone marrow and is thought to be involved in liver development. ANKRD17 localizes to the cytoplasm and the nucleus. ANKRD17 exists as five alternatively spliced isoforms that are encoded by a gene which maps to human chromosome 4. Representing approximately 6% of the human genome, chromosome 4 contains nearly 900 genes. Notably, the Huntingtin gene, which is found to encode an expanded glutamine tract in cases of Huntington's disease, is on chromosome 4. FGFR-3 is also encoded on chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease. Chromosome 4 reportedly contains the largest gene deserts (regions of the genome with no protein encoding genes) and has one of the two lowest recombination frequencies of the human chromosomes.

Supplier: Bioss

ANKRD17 is a 2,603 amino acid protein that contains 25 ankyrin repeats and one KH domain. ANKRD17 is expressed in bone marrow and is thought to be involved in liver development. ANKRD17 localizes to the cytoplasm and the nucleus. ANKRD17 exists as five alternatively spliced isoforms that are encoded by a gene which maps to human chromosome 4. Representing approximately 6% of the human genome, chromosome 4 contains nearly 900 genes. Notably, the Huntingtin gene, which is found to encode an expanded glutamine tract in cases of Huntington's disease, is on chromosome 4. FGFR-3 is also encoded on chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease. Chromosome 4 reportedly contains the largest gene deserts (regions of the genome with no protein encoding genes) and has one of the two lowest recombination frequencies of the human chromosomes.

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The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

Supplier: Bioss

The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

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Supplier: Bioss

The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

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Supplier: Bioss

The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

Supplier: Bioss

The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Supplier: Bioss

ANKRD17 is a 2,603 amino acid protein that contains 25 ankyrin repeats and one KH domain. ANKRD17 is expressed in bone marrow and is thought to be involved in liver development. ANKRD17 localizes to the cytoplasm and the nucleus. ANKRD17 exists as five alternatively spliced isoforms that are encoded by a gene which maps to human chromosome 4. Representing approximately 6% of the human genome, chromosome 4 contains nearly 900 genes. Notably, the Huntingtin gene, which is found to encode an expanded glutamine tract in cases of Huntington's disease, is on chromosome 4. FGFR-3 is also encoded on chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease. Chromosome 4 reportedly contains the largest gene deserts (regions of the genome with no protein encoding genes) and has one of the two lowest recombination frequencies of the human chromosomes.

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Supplier: Bioss

In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

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