"E1-ClipTip"

Supplier: Bioss

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG1 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.

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: Genetex

Rabbit polyclonal antibody to BCKDHA (N-terminal)

Supplier: Genetex

pstein-Barr virus (EBV) nuclear antigen 1 (EBNA1) is an EBV antigen that is expressed in all EBVassociated malignancies. EBNA1 is known to be required for maintenance of the EBV episome, and is expressed in all forms of EBV latency. Thus, EBNA1 is supposed to play a central role in the maintenance and segregation of the episomal latent EBV genome.

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: Enzo Life Sciences

Prostanoid receptor ligand

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: 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.

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

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG1 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.

Supplier: Bioss

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG1 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.

Supplier: Bioss

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG1 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.

Supplier: Bioss

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG1 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.

Supplier: Prosci

UBE2L3 (ubiquitin-conjugating enzyme E2L 3) Antibody 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 (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.