942 Results for: "single-use assemblies"

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Biotium

Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein (Workshop VI; Code N-L036). CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb recognizes CD59 transfected cells. It is useful for study on GPI-anchored proteins, PNH and CD59 functions.

Supplier: ProSci Inc.

Swine H1N1 Nucleocapsid Protein Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments, among which the nucleocapsid protein (NP), thought to control whether mRNA or cRNA is produced. The nucleoprotein (NP), which has multiple functions during the virus life cycle, possesses regions that are highly conserved among influenza A, B, and C viruses. It was recently found several NP mutations that affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions even though a single vRNA segment was incorporated efficiently. This indicates that the respective conserved amino acids in NP may be critical for the assembly and/or incorporation of sets of eight vRNA segments.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: ProSci Inc.

The 145-2C11 monoclonal antibody reacts with mouse CD3e, the 20 kDa epsilon chain of the TCR complex. Together with the gamma and delta subunits of CD3, the epsilon subunits are involved in the assembly, trafficking, and surface expression of T-cell receptor complex. CD3 is expressed on thymocytes, mature T cells, and natural killer T cells, and the epsilon chain enhances the antigen recognition.The 145-2C11 antibody binds to the TCR complex and, depending on the conditions, initiates T cells activation, proliferation, and apoptosis. The soluble antibody seems to block lysis of target cells by antigen-specific cytotoxic T lymphocytes. The 145-2C11 antibody does not cross-react with the rat leukocytes, and it is used as a phenotypic marker for mouse T lymphocytes.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: ProSci Inc.

AP2M1 Antibody: The heterotetrameric coat assembly protein complex, also known as the adaptor-related protein complex 2 (AP-2), belongs to the adaptor complexes medium subunits family. The mu 1 subunit of the AP-2 complex (AP2M1) is required for the activity of a vacuolar ATPase, which is responsible for proton pumping occurring in the acidification of endosomes and lysosomes. AP2M1 has also been shown to associate with the HIV-1 protein Nef, suggesting that Nef may use AP-2 complex to enhance the rate of endocytosis of both CD4 and class I MHC. AP2M1 may also play an important role in regulating the intracellular trafficking and function of cytotoxic T-lymphocyte associated (CTLA)-4 protein. At least two isoforms of AP2M1 are known to exist.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localisation at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).

Supplier: Bioss

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).