5766 Results for: "Ligases"

Supplier: Genetex

Rabbit Polyclonal antibody to Ligase 1 (ligase I DNA ATP-dependent) Purity: Protein G purified Species Reactivity: Human Tested Applications: WB Pkg Size: 200 ul

Supplier: Antibodies.com

Mouse monoclonal [1A9] antibody to DNA Ligase 1 for WB, ELISA and IP with samples derived from Human, Mouse, Rat and Bovine.

Supplier: Abcam

Rabbit Polyclonal DNA Ligase III/LIG3 antibody. Suitable for WB, IP and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Recombinant Fragment Protein within Human LIG3.

Supplier: New England Biolabs (NEB)

Instant Sticky-end Ligase Master Mix is a ready-to-use 2X solution of T4 DNA ligase and a proprietary ligation enhancer in an optimized reaction buffer.

Supplier: New England Biolabs (NEB)

T4 RNA Ligase 2, truncated KQ (T4 Rnl2tr R55K, K227Q) specifically ligates the preadenylated 5´ end of DNA or RNA to the 3´ OH end of RNA.

Supplier: Rockland Immunochemical

DNA Ligase T4 Molecular Biology Grade

Supplier: Genetex

Goat polyclonal antibody to DNA ligase I

Supplier: Promega Corporation

For ligation of DNA ends.

Supplier: Abcam

Rabbit Recombinant Monoclonal DNA Ligase IV/LIG4 antibody. Suitable for WB, ICC/IF, IHC-P and reacts with Human samples. Cited in 14 publications.

Supplier: Abcam

Rabbit Recombinant Monoclonal DNA Ligase IV/LIG4 antibody. BSA and Azide free. Suitable for WB, ICC/IF, IHC-P and reacts with Human samples.

Supplier: Abcam

Rabbit Polyclonal DNA Ligase III/LIG3 antibody. Suitable for WB, IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human LIG3 aa 100-450.

Supplier: Abcam

Rabbit Polyclonal DNA Ligase III/LIG3 antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human LIG3 aa 750-1000.

Supplier: Abcam

Rabbit Recombinant Monoclonal DNA Ligase III/LIG3 antibody. Suitable for Flow Cyt (Intra), IHC-P, IP, ICC/IF, WB and reacts with Human, Mouse, Rat samples.

Supplier: New England Biolabs (NEB)

New England Biolabs supplies a 10X reaction buffer with all of its enzymes

Supplier: New England Biolabs (NEB)

New England Biolabs supplies a 10X reaction buffer with all of its enzymes

Supplier: Abcam

Rabbit Recombinant Monoclonal DNA Ligase III/LIG3 antibody. BSA and Azide free. Suitable for Flow Cyt (Intra), IHC-P, IP, ICC/IF, WB and reacts with Human, Mouse, Rat samples.

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Bon Opus Biosciences

Bon Opus Biosciences offers quality recombinant proteins products covering a broad collection of cytokines, enzymes, diagnostic and detection reagents, and other protein-related products

Supplier: Genetex

Rabbit polyclonal antibody to DNA ligase I (ligase I, DNA, ATP-dependent)

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Sino Biological

Produced in rabbits immunized with purified, recombinant Escherichia coli T4 DNA ligase. Total IgG was purified by Protein A affinity chromatography.

Supplier: New England Biolabs (NEB)

New England Biolabs supplies a 10X reaction buffer with all of its enzymes

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Genetex

Mouse monoclonal [10H5] to DNA ligase I

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Bioss

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Supplier: Genetex

Mouse polyclonal to DNA ligase I

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.