5889 Results for: "Ligases"

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: Genetex

Rabbit Polyclonal antibody to UBE3A (ubiquitin protein ligase E3A)

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 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

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

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

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: Novus Biologicals

The RNF12 Antibody from Novus Biologicals is a rabbit polyclonal antibody to RNF12. This antibody reacts with human. The RNF12 Antibody has been validated for the following applications: Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.

Supplier: Prosci

Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination.

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

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: Biosensis

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. 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. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

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

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: Promega Corporation

T4 DNA Ligase and buffer combination for rapid (5-minute) ligations.

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

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: Prosci

Mahogunin (MGRN1) is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro.Mahogunin (MGRN1) is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro.

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

Supplier: Rockland Immunochemical

SMURF2 (SMAD ubiquitin regulatory factor 2) is a negative regulator of TGF-beta signaling (1). SMURF1 and SMURF2 are members of HECT domain E3 ubiquitin ligase which are involved in the enzymatic reactions of the Ub conjugating pathway (1,2). SMURF2 is widely expressed and was initially identified as an inhibitor of TGF-beta/BMP signaling by targeting R-Smads and TGF type I receptor for ubiquitination and degradation (3). Studies have shown that SMURF2 functions as a tumor suppressor by maintaining genomic stability through targeting RNF20 (3). SMURF2 associates constitutively with SMAD7 (4).

Supplier: Bioss

The TRIAD3 gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.

Supplier: Novus Biologicals

The TTLL12 Antibody from Novus Biologicals is a rabbit polyclonal antibody to TTLL12. This antibody reacts with human. The TTLL12 Antibody has been validated for the following applications: Western Blot, Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.

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: 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

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 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.