81664 Results for: "PfuUltra II Fusion HS DNA Polymerase"

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Replication factor C (RFC) is an essential DNA polymerase accessory protein that is required for numerous aspects of DNA metabolism, including DNA replication, DNA repair and telomere metabolism. RFC is a heteropentameric complex that recognizes a primer on a template DNA, binds to a primer terminus and loads proliferating cell nuclear antigen (PCNA) onto DNA at primer-template junctions in an ATP-dependent reaction. All five of the RFC subunits share a set of related sequences (RFC boxes) that include nucleotide-binding consensus sequences. Four of the five RFC genes (including RFC1, RFC2, RFC3 and RFC4) have consensus ATP-binding motifs. The small RFC proteins, RFC2, RFC3, RFC4 and RFC5, interact with Rad24, whereas the RFC1 subunit does not. RFC1 is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during FAS-mediated apoptosis. In addition, phosphorylation of the PCNA binding domain of RFC1 by Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) inhibits DNA synthesis. The human RFC1 gene maps to chromosome 4p14 and encodes the RFC1 subunit.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

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. These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors. Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation. Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity.

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: Bioss

Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery.

Supplier: ENZO LIFE SCIENCES

Mammalian apurinic/apyrimidinic (AP) endonuclease (APE1; APEX; HAP1; Ref-1) is a multifunctional, bipartite enzyme that belongs to the class II AP endonucleases and that plays an important role in numerous, cellular functions, like repairing abasic sites (loss of purine or pyrimidine base) in DNA, regulating the redox state of other proteins that play roles in oxidative signalling, transcription factor regulation (Fos, Jun, NF-κ B, Myb, HIF-1α, CREB, Pac), cell cycle control (p53) and apoptosis. APE1 initiates the DNA base excision repair (BER) by cleaving the DNA immediately adjacent to the 5’ of an AP site to produce a hydroxyl group at the 3’ terminus of an unmodified nucleotide upstream of the nick and a 5’-deoxyribose phosphate moiety downstream. The product of APE1 is further processed by DNA polymerase β to release 5’-deoxyribose phosphate with its intrinsic lyase activity. The nicked DNA is then sealed by DNA ligase I or DNA ligaseIII/XRCC1 to complete this repair process. In addition to the AP endonuclease activity, APE1 also possesses a 3’-5’ DNA exonuclease activity, a 3’-phosphodiesterase activity, a 3’-phosphatase activity, and a RNase H activity. It has been shown that APE1 is capable of excision L-configuration deoxyribonucleoside analogs from the 3’ termini of DNA. Human APE1 gene is located on chromosome 14q 11.2-12.

Supplier: Bioss

Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

Supplier: FINNZYMES REAGENTS

Phire® Hot Start II DNA Polymerase is faster, extremely robust, and capable of amplifying long DNA fragments with high yields. Phire® Hot Start II DNA Polymerase incorporates a dsDNA-binding domain which allows short extension times (10 to 15 s/kb), improves yields, and increases fidelity 2-fold compared to Taq DNA polymerase. In addition, the Hot Start technology allows complete reactivation of the enzyme in “zero-time” at standard cycling temperatures. This combination of features makes the polymerase an ideal solution for routine and high throughput PCR applications. Phire® Hot Start II DNA Polymerase delivers superior performance in conventional thermal cyclers as well as in fast instruments, such as the Piko® Thermal Cycler.

Supplier: Bioss

Replication factor C (RFC) is an essential DNA polymerase accessory protein that is required for numerous aspects of DNA metabolism, including DNA replication, DNA repair and telomere metabolism. RFC is a heteropentameric complex that recognizes a primer on a template DNA, binds to a primer terminus and loads proliferating cell nuclear antigen (PCNA) onto DNA at primer-template junctions in an ATP-dependent reaction. All five of the RFC subunits share a set of related sequences (RFC boxes) that include nucleotide-binding consensus sequences. Four of the five RFC genes (including RFC1, RFC2, RFC3 and RFC4) have consensus ATP-binding motifs. The small RFC proteins, RFC2, RFC3, RFC4 and RFC5, interact with Rad24, whereas the RFC1 subunit does not. RFC1 is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during FAS-mediated apoptosis. In addition, phosphorylation of the PCNA binding domain of RFC1 by Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) inhibits DNA synthesis. The human RFC1 gene maps to chromosome 4p14 and encodes the RFC1 subunit.

Supplier: Bioss

Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

Supplier: Bioss

Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

Supplier: Bioss

Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

Supplier: Bioss

Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

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. These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors. Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation. Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity.

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

Supplier: Bioss

This gene encodes a nuclear phosphoprotein that plays a role in maintaining genomic stability, and it also acts as a tumor suppressor. The encoded protein combines with other tumor suppressors, DNA damage sensors, and signal transducers to form a large multi-subunit protein complex known as the BRCA1-associated genome surveillance complex (BASC). This gene product associates with RNA polymerase II, and through the C-terminal domain, also interacts with histone deacetylase complexes. This protein thus plays a role in transcription, DNA repair of double-stranded breaks, and recombination. Mutations in this gene are responsible for approximately 40% of inherited breast cancers and more than 80% of inherited breast and ovarian cancers. Alternative splicing plays a role in modulating the subcellular localization and physiological function of this gene. Many alternatively spliced transcript variants, some of which are disease-associated mutations, have been described for this gene, but the full-length natures of only some of these variants has been described. A related pseudogene, which is also located on chromosome 17, has been identified. [provided by RefSeq, May 2009].

Supplier: Bioss

This gene encodes a nuclear phosphoprotein that plays a role in maintaining genomic stability, and it also acts as a tumor suppressor. The encoded protein combines with other tumor suppressors, DNA damage sensors, and signal transducers to form a large multi-subunit protein complex known as the BRCA1-associated genome surveillance complex (BASC). This gene product associates with RNA polymerase II, and through the C-terminal domain, also interacts with histone deacetylase complexes. This protein thus plays a role in transcription, DNA repair of double-stranded breaks, and recombination. Mutations in this gene are responsible for approximately 40% of inherited breast cancers and more than 80% of inherited breast and ovarian cancers. Alternative splicing plays a role in modulating the subcellular localization and physiological function of this gene. Many alternatively spliced transcript variants, some of which are disease-associated mutations, have been described for this gene, but the full-length natures of only some of these variants has been described. A related pseudogene, which is also located on chromosome 17, has been identified. [provided by RefSeq, May 2009].

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).

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 the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).