5787 Results for: "Ligases"

Supplier: Bioss

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein 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

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein 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

Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.

Supplier: Bioss

Probable E3 ubiquitin-protein ligase that may play a role in angiogenesis. May also have an ATPase activity.

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: Boster Biological Technology

Rabbit IgG polyclonal antibody for E3 SUMO-protein ligase PIAS4(PIAS4) detection. Tested with WB in Human;Mouse;Rat.

Supplier: Bioss

Probable E3 ubiquitin-protein ligase that may play a role in angiogenesis. May also have an ATPase activity.

Supplier: Bioss

PJA2, also known as E3 ubiquitin-protein ligase praja-2, RNF131 (ring finger protein 131) or Neurodap1, is a 708 amino acid protein that contains one ring-type zinc finger and exists as two alternatively spliced isoforms. Significantly conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, PJA2 shares 52% identity with PJA1, which is involved in protein ubiquitination in brain and may play a role in X-linked mental retardation. Encoded by a gene that maps to human chromosome 5q21.3, PJA2 localizes to both endoplasmic reticulum and Golgi apparatus membranes. Participating in E2-dependent, E3 ubiquitin-protein ligase activity, PJA2 binds to a variety of E2s and interacts with ubiquitin-conjugating enzymes, such as UBE2D2, in vitro.

Supplier: Bioss

E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. 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. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids.

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: Boster Biological Technology

Rabbit IgG polyclonal antibody for Long-chain-fatty-acid--CoA ligase 5(ACSL5) detection. Tested with WB in Human;Mouse;Rat.

Supplier: Bioss

Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.

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

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

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

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: Boster Biological Technology

Rabbit IgG polyclonal antibody for Long-chain-fatty-acid--CoA ligase 3(ACSL3) detection. Tested with WB in Human.

Supplier: Bioss

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein 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

MARCH4, an E3 ubiquitin protein ligase, may mediate ubiquitination of MHC I and CD4, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin protein 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 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-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: Genetex

Ubiquitin protein ligase E3 component n-recognin 7 (putative) Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human Tested Applications: ICC/IF, WB Pkg Size: 100 ul

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 mediates polyubiquitination of CD4. 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. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids.

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: 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

The protein encoded by this gene is a type I transmembrane protein that localizes to the endocytic pathway. This protein contains a RING zinc-finger motif and has been shown to possess E3 ubiquitin ligase activity. Expression of this gene in retrovirally transduced T cell hybridoma significantly inhibits activation-induced IL2 and IL4 cytokine production. Induced expression of this gene was observed in anergic CD4(+) T cells, which suggested a role in the induction of anergic phenotype. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008].