"Ligases"

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.

Supplier: Prosci

TIP120A functions as a negative regulator of SCF E3 ubiquitin ligases and may modulate other cullin ligases in a similar fashion.

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.

Supplier: VWR International

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

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.

Supplier: VWR International

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

Supplier: VWR International

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

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

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). MARCH2 (membrane-associated ring finger (C3HC4) 2), also known as RNF172 or HSPC240, is a 246 amino acid multi-pass membrane protein that localizes to the endoplasmic reticulum and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, MARCH2 functions as an E3 ubiquitin-protein ligase that is thought to mediate the ubiquitination and subsequent degradation of CD71 and B7-2 and may be involved in endosomal protein trafficking.

Supplier: VWR International

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