1466 Results for: "E1-ClipTip"

Supplier: Bioss

E2-like enzyme involved in autophagy and mitochondrial homeostasis. Catalyzes the conjugation of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to phosphatidylethanolamine (PE). PE-conjugation to ATG8-like proteins is essential for autophagy. Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3.

Supplier: Bioss

E2-like enzyme involved in autophagy and mitochondrial homeostasis. Catalyzes the conjugation of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to phosphatidylethanolamine (PE). PE-conjugation to ATG8-like proteins is essential for autophagy. Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3.

Supplier: Bioss

Cyclin E is a regulatory subunit of Cdk2 and controls G1 / S transition during the mammalian cell cycle. Multiple isoforms of Cyclin E are only expressed in tumors but not in normal tissue, suggesting a post transcriptional regulation of Cyclin E. in vitro analyses indicated that these truncated variant isoforms of Cyclin E are able to phosphorylate histone H1. Alterations in the Cyclin E protein have been implicated as indicators of worse prognosis in various cancers.

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 E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008].

Supplier: Bioss

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

Supplier: Bioss

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Supplier: Bioss

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner. TRIP13 is a transcription factor that interacts with the ligand binding domain of the thyroid receptor (TR) as well as a variety of target genes including human papilloma virus type 16 (HPV16) E1. Unlike most TRIP proteins which function only in the presence of hormones, TRIP13 does not require the presence of thyroid hormone to interact with TR. The association of TRIP13 with (HPV16) E1 suggests that TRIP13 may have tumour suppressor gene function. TRIP13 is a 432 amino acid protein with 2 different isoforms produced by alternative splicing.

Supplier: Bioss

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner. TRIP13 is a transcription factor that interacts with the ligand binding domain of the thyroid receptor (TR) as well as a variety of target genes including human papilloma virus type 16 (HPV16) E1. Unlike most TRIP proteins which function only in the presence of hormones, TRIP13 does not require the presence of thyroid hormone to interact with TR. The association of TRIP13 with (HPV16) E1 suggests that TRIP13 may have tumor suppressor gene function. TRIP13 is a 432 amino acid protein with 2 different isoforms produced by alternative splicing.

Supplier: Bioss

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner. TRIP13 is a transcription factor that interacts with the ligand binding domain of the thyroid receptor (TR) as well as a variety of target genes including human papilloma virus type 16 (HPV16) E1. Unlike most TRIP proteins which function only in the presence of hormones, TRIP13 does not require the presence of thyroid hormone to interact with TR. The association of TRIP13 with (HPV16) E1 suggests that TRIP13 may have tumor suppressor gene function. TRIP13 is a 432 amino acid protein with 2 different isoforms produced by alternative splicing.

Supplier: Abcam

Rabbit monoclonal [EPR11098] to PDHA1.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

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

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 E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner. TRIP13 is a transcription factor that interacts with the ligand binding domain of the thyroid receptor (TR) as well as a variety of target genes including human papilloma virus type 16 (HPV16) E1. Unlike most TRIP proteins which function only in the presence of hormones, TRIP13 does not require the presence of thyroid hormone to interact with TR. The association of TRIP13 with (HPV16) E1 suggests that TRIP13 may have tumour suppressor gene function. TRIP13 is a 432 amino acid protein with 2 different isoforms produced by alternative splicing.

Supplier: US Biological

Anti-CREG1 Mouse monoclonal antibody [clone: 1B7]

Supplier: Bioss

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.

Supplier: Bioss

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

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 E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner. TRIP13 is a transcription factor that interacts with the ligand binding domain of the thyroid receptor (TR) as well as a variety of target genes including human papilloma virus type 16 (HPV16) E1. Unlike most TRIP proteins which function only in the presence of hormones, TRIP13 does not require the presence of thyroid hormone to interact with TR. The association of TRIP13 with (HPV16) E1 suggests that TRIP13 may have tumor suppressor gene function. TRIP13 is a 432 amino acid protein with 2 different isoforms produced by alternative splicing.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. in vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.

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: ENZO LIFE SCIENCES

Ubiquitin Activating Kit for activation of ubiquitin for use in ubiquitinylation experiments. The kit provides the means of generating thioester linked, activated ubiquitin-E1 conjugates, utilising the first step in the ubiquitin cascade, for investigation of ubiquitin activation, subsequent ubiquitin transfer to/interaction with E2 conjugating enzymes, and their use in the ubiquitinylation of E3 ligases and target substrate proteins. Ubiquitin antibody provided allows high sensitivity detection of ubiquitin and ubiquitin-conjugates.

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

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).