"E1-ClipTip"

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2J2 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.

Supplier: Bioss

Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.

Supplier: Bioss

Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 R2 (UBE2R2) is a modification enzyme that belongs to the ubiquitin-conjugating enzyme family. UBE2R2 is involved in cell growth and transformation. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2R2 catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. It may be involved in degradation of katenin.

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). The first step in the ubiquitination process requires the ATP-dependent activation of the ubiquitin C-terminus and the assembly of multi-ubiquitin chains by the E1 enzyme. The ubiquitin chain is then conjugated to the E2 enzyme to generate an intermediate ubiquitin-E2 complex. The E3 enzyme then catalyzes the transfer of ubiquitin from E2 to the appropriate protein substrate, thereby targeting that substrate for degradation. A wide range of enzymes facilitate this proteolytic ubiquitin pathway, one of which is UBE2E2 (also known as UBCH8 in human), which functions as an E2 enzyme and catalyzes the ATP-dependent covalent attachment of ubiquitin to target proteins, thereby playing an important role in protein degradation.

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). The first step in the ubiquitination process requires the ATP-dependent activation of the ubiquitin C-terminus and the assembly of multi-ubiquitin chains by the E1 enzyme. The ubiquitin chain is then conjugated to the E2 enzyme to generate an intermediate ubiquitin-E2 complex. The E3 enzyme then catalyzes the transfer of ubiquitin from E2 to the appropriate protein substrate, thereby targeting that substrate for degradation. A wide range of enzymes facilitate this proteolytic ubiquitin pathway, one of which is UBE2E2 (also known as UBCH8 in human), which functions as an E2 enzyme and catalyzes the ATP-dependent covalent attachment of ubiquitin to target proteins, thereby playing an important role in protein degradation.

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE3B is a member of the E3 ubiquitin-conjugating enzyme family. UBE3B may interact with other proteins and play a role in stress response.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E3 ubiquitin-conjugating enzyme family. The encoded protein may interact with other proteins and play a role in stress response. Alternatively spliced transcript variants encoding the same protein isoform have been identified for this gene.

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). The first step in the ubiquitination process requires the ATP-dependent activation of the ubiquitin C-terminus and the assembly of multi-ubiquitin chains by the E1 enzyme. The ubiquitin chain is then conjugated to the E2 enzyme to generate an intermediate ubiquitin-E2 complex. The E3 enzyme then catalyzes the transfer of ubiquitin from E2 to the appropriate protein substrate, thereby targeting that substrate for degradation. A wide range of enzymes facilitate this proteolytic ubiquitin pathway, one of which is UBE2E2 (also known as UBCH8 in human), which functions as an E2 enzyme and catalyzes the ATP-dependent covalent attachment of ubiquitin to target proteins, thereby playing an important role in protein degradation.

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). The first step in the ubiquitination process requires the ATP-dependent activation of the ubiquitin C-terminus and the assembly of multi-ubiquitin chains by the E1 enzyme. The ubiquitin chain is then conjugated to the E2 enzyme to generate an intermediate ubiquitin-E2 complex. The E3 enzyme then catalyzes the transfer of ubiquitin from E2 to the appropriate protein substrate, thereby targeting that substrate for degradation. A wide range of enzymes facilitate this proteolytic ubiquitin pathway, one of which is UBE2E2 (also known as UBCH8 in human), which functions as an E2 enzyme and catalyzes the ATP-dependent covalent attachment of ubiquitin to target proteins, thereby playing an important role in protein degradation.

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2J1 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system.

Supplier: Enzo Life Sciences

Prostanoid receptor ligand.

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2I is a member of the E2 ubiquitin-conjugating enzyme family.

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2C is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for the destruction of mitotic cyclins and for cell cycle progression. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for the destruction of mitotic cyclins and for cell cycle progression. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.

Supplier: Bioss

Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.

Supplier: Bioss

Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 B (UBE2B) is a member of the ubiquitin-conjugating enzyme family. UBE2B accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It is shown that UBE2B interacts with RAD18, UBR2, and WAC. UBE2B is required for post-replicative DNA damage repair. Additional, UBE2B plays a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.