5889 Results for: "Ligases"

Supplier: Prosci

HACE1 contains 6 ANK repeats and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. HACE1 is an E3 ubiquitin-protein ligase that may function in cellular proteins degradation.

Supplier: Bioss

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.Tissue specificity: Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.

Supplier: Bioss

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, TOMM2, USP3, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by the ubiquitination of mitochondrial proteins such as TOMM2, RHOT1/MIRO1 and USP3 (PubMed:24896179). Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.

Supplier: Bioss

LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.

Supplier: Genetex

Rabbit Polyclonal antibody to ARIH2 (E3 ubiquitin-protein ligase ARIH2)

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, TOMM2, USP3, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by the ubiquitination of mitochondrial proteins such as TOMM2, RHOT1/MIRO1 and USP3 (PubMed:24896179). Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Bioss

Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 C (UBE2C) is a 179 amino acid enzyme that belongs to the Ubiquitin-Conjugating Enzyme family. UBE2C is highly expressed in tumor tissues and at low levels in most adult normal tissues. UBE2C is required for the destruction of mitotic cyclins and for cell cycle progression. UBE2C accepts Ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), which has E3 ubiquitin ligase activity, and targets for destruction substrates from the preceding mitosis (Cyclin A, Cyclin B, Securin, Geminin).

Supplier: Bioss

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

Supplier: Bioss

RNF160 may function as an E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. MARCH10 (membrane-associated ring finger (C3HC4) 10), also known as RNF190 (ring finger protein 190) or MARCH-X, is an 808 amino acid protein with one RING-CH-type zinc finger domain. MARCH10 may function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

TRIM36 (tripartite motif-containing 36), also known as RNF98 (RING finger protein 98), HAPRIN (haploid germ cell-specific RBCC protein) or RBCC728, is a 728 amino acid protein that belongs to the TRIM/RBCC (Ring finger, B box, coiled-coil) family. Predominantly expressed in prostate, testis and brain with weak expression in heart, kidney and lung, TRIM36 contains two B box-type zinc fingers, a SPRY domain, a coiled-coil domain, a fibronectin type-III domain and a RING-type zinc finger; a motif that has zinc-chelating activity and is involved in mediating protein-protein and protein-DNA interactions. Localizing to the cytoplasm and the acrosomal region of germ cells and mature sperm, TRIM36 is believed to play a role in the acrosome reaction and fertilization. In addition, TRIM36 is overexpressed in prostate cancer, suggesting a possible role for TRIM36 in prostate tumorigenesis.

Supplier: Bioss

RNF160 may function as an E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

Supplier: Bioss

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

Supplier: Bioss

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

Supplier: Bioss

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.Tissue specificity: Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis.

Supplier: Bioss

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.

Supplier: Rockland Immunochemical

RNF20 is an E3 ubiquitin ligase that regulates chromosome structure by monoubiquitinating histone H2B. RNF20 selectively suppresses the expression of some genes such as several protooncogenes and growth-related genes, including many genes that are induced by epidermal growth factor by interfering with chromatin recruitment of transcription elongation factor SII (TFIIS). In contrast, RNF20 also positively regulates the p53 tumor suppressor as well as numerous histone H2A and H2B genes. Together with the deubiquitinase USP44, RNF20 regulates stem cell differentiation by modulating H2B monoubiquitination.

Supplier: Bioss

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

Supplier: Bioss

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, TOMM2, USP3, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by the ubiquitination of mitochondrial proteins such as TOMM2, RHOT1/MIRO1 and USP3 (PubMed:24896179). Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.

Supplier: Bioss

The RING finger motif is a specialized DNA-binding zinc finger domain found in many transcriptional regulatory proteins. The ring finger protein (RNF) family includes any protein containing the signature RING finger motif. RNF8 is a ubiquitously expressed nuclear RING finger protein that acts as an E3 ubiquitin-protein ligase. It is required for the ubiquitination of some nuclear proteins and promotes their subsequent degradation. The heterodimeric ubiquitin-conjugating enzyme UBC13 interacts with RNF8, and they co-localize in the nucleus. RNF8 may regulate mediation of UBC13 polyubiquitylation by elongating the ubiquitin chains. RNF8 also binds to Retinoid X receptor alpha (RXR?, a member of the steroid hormone receptor superfamily. It increases RXR?mediated transactivation of the RXR?responsive element (RXRE) promoter in a dose-dependent manner, suggesting that RNF8 is a regulator of RXR?mediated transcriptional activity.

Supplier: Rockland Immunochemical

Parkinson’s disease (PD) is a neurodegenerative disease whose symptoms include tremors, rigidity, bradykinesia, and postural instability (1). Mutations in the PARK2 gene are known to cause Parkinson disease and autosomal recessive juvenile Parkinson disease (2). The PARK2 protein is a component of a multiprotein E3 ubiquitin ligase complex that mediates the targeting of substrate proteins for proteasomal degradation (3). Recent studies have suggested that PARK2 expression reduces the mitochondrial accumulation of the apoptosis protein Bax under basal conditions and directly ubiquitinates Bax, thereby promoting cell survival (4).