5792 Results for: "Ligases"

Supplier: Bioss

MARCH6 (Membrane associated RING finger protein 6) belongs to the MARCH family, which contains at least seven membrane associated RING-CH (MARCH)proteins. MARCH proteins are E3 ubiquitin ligases and are located to subcellular membranes.

Supplier: Bioss

E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of PCNP. May participate in methylation-dependent transcriptional regulation. Important for G1/S transition. Overexpression causes G1 phase cell arrest.

Supplier: Boster Biological Technology

Rabbit IgG polyclonal antibody for RNF43 detection. Tested with WB, Direct ELISA in Human;Mouse;Rat.

Supplier: Bioss

RNF133 contains a RING finger domain, a motif known to be involved in protein-protein and protein-DNA interactions. This gene has no intron. RNF133 may have E3 ubiquitin-protein ligase activity.

Supplier: Genetex

STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human Tested Applications: IHC-P, WB Pkg Size: 100 ul

Supplier: Bioss

E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of PCNP. May participate in methylation-dependent transcriptional regulation. Important for G1/S transition. Overexpression causes G1 phase cell arrest.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

MARCH6 (Membrane associated RING finger protein 6) belongs to the MARCH family, which contains at least seven membrane associated RING-CH (MARCH)proteins. MARCH proteins are E3 ubiquitin ligases and are located to subcellular membranes.

Supplier: Bioss

E3 ubiquitin-protein ligase. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway.

Supplier: Bioss

Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.

Supplier: Rockland Immunochemical

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner (1). TRIP12 (thyroid hormone receptor interactor 12) is an ATP-dependent E3 ubiquitin ligase involved in the human ubiquitin fusion degradation (UFD) pathway and also modulates the NEDD8 pathway (2,3). TRIP12 contains one WWE domain and a single HECT (E6AP-type E3 ubiquitin-protein ligase) domain suggested to contain a noncovalent ubiquitin-binding site (4). TRIP12 acts as a key regulator of DNA damage response and the ubiquitin ligase activity of TRIP12 is essential for mouse development (5).

Supplier: Abnova

TOPORS polyclonal antibody (A01), Mouse polyclonal antibody raised against a partial recombinant TOPORS, Size: 50ul

Supplier: Bioss

The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.

Supplier: Bioss

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

Supplier: Bioss

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

Supplier: New England Biolabs (NEB)

The Quick Ligation Kit enables ligation of cohesive end or blunt end DNA fragments in 5 minutes at room temperature

Supplier: Bioss

E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.

Supplier: Bioss

E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of PCNP. May participate in methylation-dependent transcriptional regulation. Important for G1/S transition. Overexpression causes G1 phase cell arrest.

Supplier: Bioss

E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.

Supplier: Prosci

E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. 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

E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.

Supplier: Bioss

E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.

Supplier: Bioss

Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.

Supplier: Bioss

The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. 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. ZNRF1 (zinc and ring finger 1), also known as NIN283, is a 227 amino acid protein that contains one RING-type zinc finger and localizes to the lysosome and the endosome, as well as to cytoplasmic vesicles and the peripheral membrane. Expressed primarily in nervous system tissue, but also present in testis and thymus, ZNRF1 functions as an E3 ubiquitin-protein ligase that is thought to play a role in the establishment and maintenance of neuronal plasticity. Multiple isoforms of ZNRF1 exist due to alternative splicing events.

Supplier: Bioss

Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.

Supplier: Prosci

E3 ubiquitin-protein ligase. It seems to utilize UBE2E1. In vitro, generates polyubiquitin chains via non-canonical lysine residues suggesting that it is not involved in tagging substrates for proteosomal degradation (By similarity).

Supplier: Bioss

RNF20 is an E3 ubiquitin ligase protein that mediates monoubiquitination of histone H2B and the methylation of histone H3. It forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a central role in histone code and gene regulation. It is required for transcriptional activation of Hox genes. It is recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator.