793 Results for: "E1-ClipTip"

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

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

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

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

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). MARCH9 (membrane-associated ring finger (C3HC4) 9), also known as RNF179, is a 346 amino acid multi-pass membrane protein that localizes to the golgi apparatus and contains one RING-CH-type zinc finger. Expressed ubiquitously, MARCH9 exists as a homodimer and functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to promote the degradation of target proteins, such as CD4 and MHC-I. Multiple isoforms of MARCH9 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). UBC13, also known as UBE2N or BLU, is a 152 amino acid member of the E2 ubiquitin-conjugating enzyme family. Existing as a heterodimer with Mms2 (also known as UBE2V2), UBC13 catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process that does not lead to proteasomal degradation. Additionally, UBC13 mediates the transcription of several target genes and is thought to play a role in cell cycle progression, cellular differentiation and DNA repair mechanisms that ensure cell survival after DNA damage.

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. 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

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

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). MARCH2 (membrane-associated ring finger (C3HC4) 2), also known as RNF172 or HSPC240, is a 246 amino acid multi-pass membrane protein that localizes to the endoplasmic reticulum and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, MARCH2 functions as an E3 ubiquitin-protein ligase that is thought to mediate the ubiquitination and subsequent degradation of CD71 and B7-2 and may be involved in endosomal protein trafficking.

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). MARCH2 (membrane-associated ring finger (C3HC4) 2), also known as RNF172 or HSPC240, is a 246 amino acid multi-pass membrane protein that localizes to the endoplasmic reticulum and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, MARCH2 functions as an E3 ubiquitin-protein ligase that is thought to mediate the ubiquitination and subsequent degradation of CD71 and B7-2 and may be involved in endosomal protein trafficking.

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 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

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

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

Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 (PubMed:21976273).

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: Biotium

This MAb is specific to SUMO-1 and shows no cross-reaction with either SUMO-2 or SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2, and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1 protein localizes to the nuclear membrane.

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: 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: 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: 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: 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: 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). MARCH2 (membrane-associated ring finger (C3HC4) 2), also known as RNF172 or HSPC240, is a 246 amino acid multi-pass membrane protein that localizes to the endoplasmic reticulum and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, MARCH2 functions as an E3 ubiquitin-protein ligase that is thought to mediate the ubiquitination and subsequent degradation of CD71 and B7-2 and may be involved in endosomal protein trafficking.

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.