125338 Results for: "The GeneMorph II Random Mutagenesis Kits"

Supplier: Bioss

DNA polymerase lambda (pol Kappa), also designated DNA polymerase Kappa or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol Kappa is a member of the DNA polymerase type-X family. Pol Kappa extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol Kappa may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol Kappa and thus influences the ability of pol Kappa to synthesize DNA.

Supplier: Cytiva

PCR nucleotide mix dNTP set (2 mM, 10 mM, or 25 mM each A,C,G,T) for amplification, dideoxy sequencing, labelling, mutagenesis, cDNA synthesis, and expression profiling.

Supplier: Bioss

DNA polymerase lambda (pol Kappa), also designated DNA polymerase Kappa or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol Kappa is a member of the DNA polymerase type-X family. Pol Kappa extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol Kappa may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol Kappa and thus influences the ability of pol Kappa to synthesize DNA.

Supplier: Bioss

DNA polymerase lambda (pol Kappa), also designated DNA polymerase Kappa or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol Kappa is a member of the DNA polymerase type-X family. Pol Kappa extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol Kappa may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol Kappa and thus influences the ability of pol Kappa to synthesize DNA.

Supplier: Bioss

DNA polymerase lambda (pol lambda), also designated DNA polymerase lambda or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol lambda is a member of the DNA polymerase type-X family. Pol lambda extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol ?may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol lambda and thus influences the ability of pol ?to synthesize DNA.

Supplier: Bioss

DNA polymerase lambda (pol lambda), also designated DNA polymerase lambda or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol lambda is a member of the DNA polymerase type-X family. Pol lambda extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol ?may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol lambda and thus influences the ability of pol ?to synthesize DNA.

Supplier: Bioss

DNA polymerase lambda (pol Kappa), also designated DNA polymerase Kappa or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol Kappa is a member of the DNA polymerase type-X family. Pol Kappa extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol Kappa may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol Kappa and thus influences the ability of pol Kappa to synthesize DNA.

Supplier: Bioss

DNA polymerase lambda (pol lambda), also designated DNA polymerase lambda or Pol Beta2, is a low-fidelity polymerase which plays a role in both spontaneous and DNA damage-induced mutagenesis. Encoded by the POLL gene, pol lambda is a member of the DNA polymerase type-X family. Pol lambda extends primer-terminal mispairs opposite nondamaged DNA templates, suggesting that it may assist in extending mismatched base pairs during normal DNA replication. In addition, pol ?may play a role in the mutagenic bypass of T-T dimers. Proliferating cell nuclear antigen (PCNA), a protein essential to DNA replication, interacts with pol lambda and thus influences the ability of pol ?to synthesize DNA.

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: Bioss

DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).

Supplier: ENZO LIFE SCIENCES

Gold 525 [5(6)-Carboxyrhodamine 6G] dUTP can replace TTP in reactions in which it serves as a substrate for E. coli DNA polymerase (holoenzyme and Klenow fragment), T4 and Taq DNA polymerases, reverse transcriptase (from AMV and M-MuLV) and terminal transferase. Fluorescently labelled probes can be prepared with this fluorescent nucleotide by a variety of methods including nick translation, random prime labelling, cDNA labelling and 3’-end labelling. Probes generated by these methods are suitable for use for the identification of specific sequences by in situ hybridization procedures on fixed cells and tissues by direct fluorescence detection. Gold 525 dUTP can also be used for multicolor fluorescence labelling.

Supplier: Bioss

E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.

Supplier: ENZO LIFE SCIENCES

Cell-permeable, phosphodiesterase-resistant cGMP antagonist. Reversed NO stimulation of random migration in rabbit neutrophils. Used at 30µM to cometively inhibit 8-Br-cGMP relaxation of rabbit aortas. The product is not sterile. Resistant to nucleotide-dependent phosphodiesterases; no metabolic side effects. Significantly more lipophilic and membrane permeant as compared to cyclic GMP or Rp-cGMPS.

Supplier: Bioss

Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39.Involvement in disease:Defects in CCDC40 are the cause of primary ciliary dyskinesia type 15 (CILD15) . A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome.

Supplier: Bioss

Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39.Involvement in disease:Defects in CCDC40 are the cause of primary ciliary dyskinesia type 15 (CILD15) . A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome.

Supplier: Bioss

Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Not required for outer dynein arm complexes assembly. Required for axonemal recruitment of CCDC39.Involvement in disease:Defects in CCDC40 are the cause of primary ciliary dyskinesia type 15 (CILD15) . A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome.

Supplier: VWR Chemicals

10 ml of solution corresponds to about 0,050 g of anhydrous glucose

Supplier: Cytiva

dNTPs designed for applications requiring high purity such as amplification, dideoxy sequencing, labeling, mutagenesis, cDNA synthesis, and expression profiling.

Supplier: Cytiva

illustra™ dNTPs are high purity solutions for enzymatically sensitive applications, such as nucleic acid amplification, sequencing, labelling, mutagenesis, cDNA synthesis and expression profiling.

Supplier: Bioss

E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.

Supplier: Bioss

E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.