793 Results for: "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

Ubiquitin-Conjugating Enzyme E2 D4 (UBE2D4) is a ligase that belongs to the Ubiquitin-Conjugating Enzyme family. UBE2D4 has been proposed to participate in Ubl conjugation pathway. UBE2D4 takes part in post-translational protein modification, protein K6-linked ubiquitination, protein K11-linked ubiquitination, protein K27-linked ubiquitination, protein K29-linked ubiquitination, protein K48-linked ubiquitination, and protein K63-linked ubiquitination. UBE2D4 regulate of protein metabolic process. UBE2D4 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2D4 able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11' and 'Lys-48'-linked poly-ubiquitination.

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). MARCH3 (membrane-associated ring finger (C3HC4) 3), also known as RNF173, is a 253 amino acid multi-pass membrane protein that localizes to cytoplasmic vesicles and early endosomes and contains one RING-CH-type zinc finger. Involved in the pathway of protein modification, MARCH3 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to be involved in endosomal trafficking events.

Supplier: Proteintech

CSDE1 (Cold shock domain-containing protein E1), also known as UNR (upstream of N-ras), is an RNA-binding protein involved in the regulation of messenger RNA stability and internal initiation of translation. It is required for internal initiation of translation of human rhinovirus RNA. UNR may be involved in translationally coupled mRNA turnover. Reduced expression of UNR impairs proliferation and differentiation of erythroid blasts. Recent study found that UNR acts as a positive or negative regulator of cell death, depending on the cell type, suggesteing manipulation of UNR level may constitute a specific approach to sensitize cancer cells to anticancer treatments.

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.

Supplier: Proteintech

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. UBE2N is a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair

Supplier: Proteintech

The BCHE antibody from Proteintech is a rabbit polyclonal antibody to a fusion protein of human BCHE. This antibody recognizes human antigen. The BCHE antibody has been validated for the following applications: ELISA, WB, IHC, IF analysis.

Supplier: Prosci

UBE2N encodes 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. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.

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). ZNRF2 (zinc and ring finger 2), also known as RNF202, is a 242 amino acid peripheral membrane protein that contains one RING-type zinc finger and localizes to the lysosome, as well as the endosome and the cell junction. Expressed at high levels in brain tissue, ZNRF2 is thought to function as an E3 ubiquitin-protein ligase that may be involved in the establishment and maintenance of neuronal transmission and plasticity. Upon DNA damage, ZNRF2 is subject to phosphorylation, probably by ATR or ATM.

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). ZNRF2 (zinc and ring finger 2), also known as RNF202, is a 242 amino acid peripheral membrane protein that contains one RING-type zinc finger and localizes to the lysosome, as well as the endosome and the cell junction. Expressed at high levels in brain tissue, ZNRF2 is thought to function as an E3 ubiquitin-protein ligase that may be involved in the establishment and maintenance of neuronal transmission and plasticity. Upon DNA damage, ZNRF2 is subject to phosphorylation, probably by ATR or ATM.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Prosci

APG7 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. Another member of the autophagy family of proteins is APG7 which was identified in yeast as a ubiquitin-E1-like enzyme; this function is conserved in the mammalian homolog. In mammalian cells, APG7 is essential for autophagy conjugation systems, autophagosome formation, starvation-induced bulk degradation of proteins and organelles. It has been suggested that caspase-8 may alter APG7 levels and thus the APG7 program of autophagic cell death.

Supplier: Prosci

APG7 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. Another member of the autophagy family of proteins is APG7 which was identified in yeast as a ubiquitin-E1-like enzyme; this function is conserved in the mammalian homolog. In mammalian cells, APG7 is essential for autophagy conjugation systems, autophagosome formation, starvation-induced bulk degradation of proteins and organelles. It has been suggested that caspase-8 may alter APG7 levels and thus the APG7 program of autophagic cell death.

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). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

Supplier: Prosci

APG7 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. Another member of the autophagy family of proteins is APG7 which was identified in yeast as a ubiquitin-E1-like enzyme; this function is conserved in the mammalian homolog. In mammalian cells, APG7 is essential for autophagy conjugation systems, autophagosome formation, starvation-induced bulk degradation of proteins and organelles. It has been suggested that caspase-8 may alter APG7 levels and thus the APG7 program of autophagic cell death.

Supplier: Bioss

UBE2G2 (Ubiquitin-conjugating enzyme E2 G2), also known as UBC7, is a 165 amino acid protein involved in ubiquitin-mediated protein degradation. 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). UBE2G2 is an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitins to various proteins. Expressed throughout the body, UBE2G2 shares 100% sequence identity with its mouse counterpart and is thought to be involved in endoplasmic reticulum-associated degradation (ERAD). Two isoforms of UBE2G2 exist due to alternative splicing events.

Supplier: Bioss

UBE2G2 (Ubiquitin-conjugating enzyme E2 G2), also known as UBC7, is a 165 amino acid protein involved in ubiquitin-mediated protein degradation. 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). UBE2G2 is an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitins to various proteins. Expressed throughout the body, UBE2G2 shares 100% sequence identity with its mouse counterpart and is thought to be involved in endoplasmic reticulum-associated degradation (ERAD). Two isoforms of UBE2G2 exist due to alternative splicing events.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2C, also designated UBCH10 in human, is an E2 ubiquitin conjugating enzyme for the anaphase promoting complex (APC), which coordinates mitosis and G1 by sequentially promoting the degradation of key cell-cycle regulators. UBE2C is overexpressed in many different types of cancers and may be a potential therapeutic target.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2A (Ubiquitin-conjugating enzyme E2 A) and UBE2B (Ubiquitin-conjugating enzyme E2 B) are both Ub-conjugating enzymes that are essential to postreplication repair of UV-damaged DNA. UBE2A and UBE2B are both nuclear and cell membrane proteins that have been found to interact with Rad18.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2A (Ubiquitin-conjugating enzyme E2 A) and UBE2B (Ubiquitin-conjugating enzyme E2 B) are both Ub-conjugating enzymes that are essential to postreplication repair of UV-damaged DNA. UBE2A and UBE2B are both nuclear and cell membrane proteins that have been found to interact with Rad18.

Supplier: Bioss

E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation.

Supplier: Bioss

HCV is classified into the genus Hepacivirus of the family Flaviviridae. Like all the members of the family, HCV is an enveloped, single-stranded, positive-sense RNA virus. Its genome (about 9600 nt) is flanked at both termini by conserved, highly structured non-translated regions (NTRs) and encodes a polyprotein precursor (about 3000 aa), which is proteolytically processed by host and viral proteases to produce the structural (core, E1, E2 and p7) and non-structural (NS2, NS3, NS4A, NS4B, NS5A and NS5B) proteins of the virus. Recently, an additional protein has been identified, whose function remains unknown. NS5A is a ~56 kDa pleiotropic protein with key roles in both viral RNA replication and modulation of the physiology of the host cell. It's exact role is not currently known (2008).

Supplier: Bioss

E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires ATP-dependent activation of the Ub C-terminus and assembly of multi-Ub chains by a Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2U (ubiquitin-conjugating enzyme E2U) is a 321 amino acid E2 ubiquitin conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. Existing as two alternatively spliced isoforms, UBE2U is encoded by a gene located on human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2C, also designated UBCH10 in human, is an E2 ubiquitin conjugating enzyme for the anaphase promoting complex (APC), which coordinates mitosis and G1 by sequentially promoting the degradation of key cell-cycle regulators. UBE2C is overexpressed in many different types of cancers and may be a potential therapeutic target.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2E1 and UBE2L3, also designated UBCH6 and UBCH7 respectively in human, are E2 conjugating enzymes that interact with various proteins. Specifically, UBE2E1 interacts with the tumor suppressor protein TSSC5. UBE2L3 has been shown to mediate c-fos degradation, NF-kB maturation, human papilloma virus-mediated p53 and Myc protein degradation.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires ATP-dependent activation of the Ub C-terminus and assembly of multi-Ub chains by a Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2U (ubiquitin-conjugating enzyme E2U) is a 321 amino acid E2 ubiquitin conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. Existing as two alternatively spliced isoforms, UBE2U is encoded by a gene located on human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires ATP-dependent activation of the Ub C-terminus and assembly of multi-Ub chains by a Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2U (ubiquitin-conjugating enzyme E2U) is a 321 amino acid E2 ubiquitin conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. Existing as two alternatively spliced isoforms, UBE2U is encoded by a gene located on human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome.

Supplier: Bioss

UBE2H, also known as UBC8, UBCH, UBCH2 or E2-20K, is a 183 amino acid protein involved in ubiquitin-mediated protein degradation. 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). One of several members of the ubiquitin-conjugating enzyme family, UBE2H functions as an E2 ubiquitin-conjugating enzyme that acts to catalyze the covalent attachment of ubiquitin residues to various proteins, including Histone H2A. UBE2H shares 100% identity with its mouse counterpart and 98% identity with its frog and zebrafish homologs, suggesting a conserved function between species. Multiple isoforms of UBE2H exist due to alternative splicing events.

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). ZNRF2 (zinc and ring finger 2), also known as RNF202, is a 242 amino acid peripheral membrane protein that contains one RING-type zinc finger and localizes to the lysosome, as well as the endosome and the cell junction. Expressed at high levels in brain tissue, ZNRF2 is thought to function as an E3 ubiquitin-protein ligase that may be involved in the establishment and maintenance of neuronal transmission and plasticity. Upon DNA damage, ZNRF2 is subject to phosphorylation, probably by ATR or ATM.