919 Résultats pour : « E1-ClipTip »

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

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Proteintech

Cyclin E1 (CCNE1) is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. CCNE1, an essential cyclin activating Cdk2, regulates the G1-S phase transition of the mammalian cell division cycle. Its timing expression plays a direct role in the initiation of DNA replication , the control of histone biosynthesis, and the centrosome cycle. CCNE1 is associated with disease progression in various malignancies and is associated clinically with poor prognosis.

Supplier: Bioss

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Proteintech

NEDD8 (neural precursor cell-expressed developmentally down-regulated gene 8) is a small ubiquitin-like protein that shares 60% sequence identity and 80% homology with ubiquitin . NEDD8 is conjugated to substrate proteins in a process known as neddylation. NEDD8 forms a thioester bond with APPBP1-Uba3, the E1 enzyme. Activated NEDD8 then transfers to Ubc12, the E2 enzyme . Ultimately, E2 loaded with NEDD8 binds a substrate protein lysine residue and forms an isopeptide bond by E3 ligase .

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. UBE2D3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase.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 functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Multiple spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been determined.

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 (UBE2A) is a member of the E2 Ubiquitin-Conjugating Enzyme family. 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. UBE2A catalyzes the covalent attachment of ubiquitin to other proteins. UBE2A is required for postreplication repair of UV-damaged DNA. UBE2A Interacts with RAD18 and WAC.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

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. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Thermo Scientific

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 transcript variants encoding different isoforms have been found for this gene.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. in vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

E(rns), E1 and E2 are responsible of cell attachment and subsequent fusion of viral and cellular membrane. P7 forms a leader sequence to properly orient NS2 in the membrane. Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Proteintech

TRIP13 gene encodes thyroid receptor-interacting protein 13, that interact with thyroid hormone receptors, also known as human papillomavirus type 16 E1 protein-binding protein (16E1BP). This protein belongs to the AAA ATPase family and the PCH2 subfamily. TRIP13 gene may be one of the several playing roles in early-stage non-small cell lung cancer. TRIP13 also functions in chromosome recombination and chromosome structure development during meiosis, and it is required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. in vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

The early region (E1) of the adenovirus genome, responsible for transforming activity, is localized within the left most 11% of the viral genome and consists of two transcriptional units E1A and E1B. E1A is sufficient for partial transformation and immortalization of primary cells. E1A gene products are necessary for normal levels of transcription of the other early regions of the adenovirus genome during productive infection and are able to either activate or repress the transcription of specific cellular genes. E1A forms specific complexes with cellular proteins including p105 causing inhibition of the cell cycle inducing arresting function of p105.

Supplier: Bioss

The early region (E1) of the adenovirus genome, responsible for transforming activity, is localized within the left most 11% of the viral genome and consists of two transcriptional units E1A and E1B. E1A is sufficient for partial transformation and immortalization of primary cells. E1A gene products are necessary for normal levels of transcription of the other early regions of the adenovirus genome during productive infection and are able to either activate or repress the transcription of specific cellular genes. E1A forms specific complexes with cellular proteins including p105 causing inhibition of the cell cycle inducing arresting function of p105.

Supplier: Bioss

The early region (E1) of the adenovirus genome, responsible for transforming activity, is localized within the left most 11% of the viral genome and consists of two transcriptional units E1A and E1B. E1A is sufficient for partial transformation and immortalization of primary cells. E1A gene products are necessary for normal levels of transcription of the other early regions of the adenovirus genome during productive infection and are able to either activate or repress the transcription of specific cellular genes. E1A forms specific complexes with cellular proteins including p105 causing inhibition of the cell cycle inducing arresting function of p105.

Supplier: Bioss

E(rns), E1 and E2 are responsible of cell attachment and subsequent fusion of viral and cellular membrane. P7 forms a leader sequence to properly orient NS2 in the membrane.
Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.

Supplier: Prosci

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 T (UBE2T) is a ligase that belongs to the Ubiquitin-Conjugating Enzyme family. UBE2T accepts the ATP-dependent ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2T is able to catalyze polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. UBE2T is an important factor of the Faconi anemia pathway of DNA damage repair and, upon self-inactivation, may negatively regulate the Faconi pathway.

Supplier: Prosci

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).This gene encodes one subunit of the 2-oxoglutarate dehydrogenase complex. This complex catalyzes the overall conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA and CO (2) during the Krebs cycle. The protein is located in the mitocondrial matrix and uses thiamine pyrophosphate as a cofactor. A congential deficiency in 2-oxoglutarate dehydrogenase activity is believed to lead to hypotonia, metabolic acidosis, and hyperlactatemia.