5787 Results for: "Ligases"

Supplier: Boster Biological Technology

Leucyl tRNA synthetase /LARS Polyclonal Antibody, Host: Rabbit, Reactivity: Human, Mouse, Rat, Isotype: IgG, Immunogen: E. Coli-derived Leucyl tRNA synthetase/LARS recombinant protein (Q628-Q855, Alternative Names: LARS1, Leucine--tRNA ligase, cytoplasmic, Application: WB, Size: 100ug/vial

Supplier: Bioss

E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugatin.

Supplier: Boster Biological Technology

RNF168 Polyclonal Antibody, Host: Rabbit, Reactivity: Human, Isotype: IgG, Immunogen: E.coli-derived human RNF168 recombinant protein (Position: K5-K571), Alternative Names: RNF168, E3 ubiquitin-protein ligase RNF168, EC 6.3.2, EC 6.3.2.-, FLJ39749, Applications: WB, Size: 100ug/vial

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: Antibodies.com

Rabbit polyclonal antibody to PIAS4 for WB, IHC and ELISA with samples derived from Human and Mouse.

Supplier: Bioss

E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugatin.

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: Genetex

Purity: Purified by antigen-affinity chromatography. Species Reactivity: Mouse Tested Applications: WB Pkg Size: 100 ul

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: New England Biolabs (NEB)

KLD Enzyme Mix is a unique blend of Kinase, Ligase and DpnI enzymes.

Supplier: Genetex

Mouse Monoclonal antibody [GT7711] to Glutamine synthetase (glutamate-ammonia ligase)

Supplier: Genetex

Mouse Monoclonal antibody [GT1055] to Glutamine synthetase (glutamate-ammonia ligase)

Supplier: New England Biolabs (NEB)

ElectroLigase™ combines T4 DNA ligase and an optimized, ready-to-use 2X reaction buffer containing a proprietary ligation enhancer and no PEG.

Supplier: Bioss

MARCH5 is a member of the E3 ubiquitin-protein ligase family. This mitochonrial E3 ubiquitin-protein ligase plays an importnat role in controlling the morphology of the mitochondria. 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. MARCH5 has been shown to interact with MTFN2 and ubiquitinated forms of DRP1.

Supplier: Bioss

MARCH5 is a member of the E3 ubiquitin-protein ligase family. This mitochonrial E3 ubiquitin-protein ligase plays an importnat role in controlling the morphology of the mitochondria. 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. MARCH5 has been shown to interact with MTFN2 and ubiquitinated forms of DRP1.

Supplier: Genetex

Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human Tested Applications: WB Pkg Size: 100 ul

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: Novus Biologicals

The KAP1 Antibody (4E6) from Novus Biologicals is a mouse monoclonal antibody to KAP1. This antibody reacts with human, mouse, rat. The KAP1 Antibody (4E6) has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin, RNA Inhibition.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Bioss

MARCH5 is a member of the E3 ubiquitin-protein ligase family. This mitochonrial E3 ubiquitin-protein ligase plays an importnat role in controlling the morphology of the mitochondria. 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. MARCH5 has been shown to interact with MTFN2 and ubiquitinated forms of DRP1.

Supplier: Bioss

MARCH5 is a member of the E3 ubiquitin-protein ligase family. This mitochonrial E3 ubiquitin-protein ligase plays an importnat role in controlling the morphology of the mitochondria. 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. MARCH5 has been shown to interact with MTFN2 and ubiquitinated forms of DRP1.