793 Results for: "E1-ClipTip"

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.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®594 is a deep red fluorescent dye (Ex/Em 593/614 nm). It yields the brightest conjugates among spectrally similar dyes, and has excellent photostability.

Supplier: Bioss

Ubiquitin like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg12 and Hub1. Proteins of the second class include Parkin, RAD23 and DSK2, are designated ubiquitin domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not proteolytically processed or conjugated to other proteins. Rub1 and the corresponding human homolog NEDD8 are activated by the E1 ubiquitin activating enzyme UBA2, that forms isopeptide linkages between thio esters. NEDD8 shows 80% homology to ubiquitin. The best known targets of Rub1 modification are members of the cullin family. Cullins are subunits of an E3 ubiquitin ligase complex called the Skp1 /Cul1/Cdc53 F box (SCF). The SCF promotes transfer of ubiquitin from a ubiquitin conjugating enzyme (E2) to the target protein. Rub1 modification may regulate SCF function or localization.

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.

Supplier: Bioss

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, SUMO-2 and SUMO-3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include IkBa, MDM2, p53, PML and Ran GAP1. SUMO-2 and SUMO-3 contribute to a greater percentage of protein modification than does SUMO-1, and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates b-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

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. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.

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

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. 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). As an E2 class enzyme, UBE2W (Ubiquitin-conjugating enzyme E2 W), also known as Ubiquitin carrier protein W, is a 151 amino acid that catalyzes the conjugation of ubiquitin to proteins that are meant for lysosomal degradation. Functioning as a homodimer, UBE2W is widely expressed, with highest levels in testis. There are two isoforms of UBE2W that are produced as a result of alternative splicing 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. 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). As an E2 class enzyme, UBE2W (Ubiquitin-conjugating enzyme E2 W), also known as Ubiquitin carrier protein W, is a 151 amino acid that catalyzes the conjugation of ubiquitin to proteins that are meant for lysosomal degradation. Functioning as a homodimer, UBE2W is widely expressed, with highest levels in testis. There are two isoforms of UBE2W that are produced as a result of alternative splicing events.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. 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). As an E2 class enzyme, UBE2W (Ubiquitin-conjugating enzyme E2 W), also known as Ubiquitin carrier protein W, is a 151 amino acid that catalyzes the conjugation of ubiquitin to proteins that are meant for lysosomal degradation. Functioning as a homodimer, UBE2W is widely expressed, with highest levels in testis. There are two isoforms of UBE2W that are produced as a result of 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). 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

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

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

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

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

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

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

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

Ubiquitin like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg12 and Hub1. Proteins of the second class include Parkin, RAD23 and DSK2, are designated ubiquitin domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not proteolytically processed or conjugated to other proteins. Rub1 and the corresponding human homolog NEDD8 are activated by the E1 ubiquitin activating enzyme UBA2, that forms isopeptide linkages between thio esters. NEDD8 shows 80% homology to ubiquitin. The best known targets of Rub1 modification are members of the cullin family. Cullins are subunits of an E3 ubiquitin ligase complex called the Skp1 /Cul1/Cdc53 F box (SCF). The SCF promotes transfer of ubiquitin from a ubiquitin conjugating enzyme (E2) to the target protein. Rub1 modification may regulate SCF function or localization.

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

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

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

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

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. Ubiquitin conjugating enzyme 8 (UBC8) is an E2 enzyme involved in the ubiquitin pathway for protein degradation. Like other E2 enzymes, UBC8 forms a thioester bond with ubiquitin in an E1-dependent manner. UBC8 binds to the human homolog of Drosophila ariadne (HHARI) and UBC7-associated protein (H7-AP1) as well as double ring-finger protein (Dorfin). UBC8 is enriched in the central nervous system and interacts with Parkin, a RING-finger-containing protein implicated in the pathogenesis of familial Parkinson’s disease. Parkin shares sequence homology with other UBC8 binding proteins such as HHARI and H7-AP1.