"Ligases"

Supplier: Bioss

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein ligases accept ubiquitin from an E2 ubiquitin conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

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

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

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

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein ligases accept ubiquitin from an E2 ubiquitin conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

Supplier: Genetex

Rabbit Polyclonal antibody to RNF168 (ring finger protein 168, E3 ubiquitin protein ligase)

Supplier: VWR International

Ready-to-use enzyme-linked immunosorbent assay kits (ELISA kits).

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

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

Supplier: Bioss

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

Supplier: Bioss

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

Supplier: Bioss

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

Supplier: Bioss

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

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.