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

Supplier: Bioss

Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111).

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: FINNZYMES REAGENTS

Phusion® U DNA polymerase is a novel engineered high fidelity enzyme developed using fusion technology.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

RNA polymerase II (Pol II) is an enzyme that is composed of twelve subunits and is responsible for the transcription of protein-coding genes. Transcription initiation requires Pol II-mediated recruitment of transcription machinery to a target promoter, thereby allowing transcription to begin. The largest subunit of Pol II (referred to as RPB1 or RPB205) is a 1,840 amino acid protein that contains one C2H2-type zinc finger and a C-terminal domain comprised of several heptapeptide repeats. Although Pol II function requires the cooperation of all twelve subunits, the largest subunit conveys Pol II catalytic activity and, together with the second largest subunit, forms the active center of the Pol II enzyme. Additionally, the large subunit participates in forming the DNA-binding domain of Pol II, a groove that is necessary for transcription of the DNA template. Without proper function of the large subunit, mRNA synthesis and subsequent transcription elongation cannot occur.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

XAB2 protein (XPA binding protein 2) was first identified through its interaction with XPA, a key factor in nucleotide excision repair pathways. XAB2 therefore appears to be involved in transcription coupled DNA repair and transcription. Immunoprecipitation experiments have also demonstrated that a fraction of XAB2 interacts with the transcription coupled repair specific proteins CSA and CSB as well as with RNA polymerase II. Microinjection experiments with XAB2 resulted in the inhibition of both transcription coupled repair and transcription.

Supplier: Bioss

Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent Signalling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilisation of the complex at DNA damage sites.

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

Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent Signalling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilisation of the complex at DNA damage sites.

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.