5877 Results for: "Ligases"

Supplier: Novus Biologicals

The SARS2 Antibody from Novus Biologicals is a rabbit polyclonal antibody to SARS2. This antibody reacts with human. The SARS2 Antibody has been validated for the following applications: Western Blot, Immunohistochemistry, Immunohistochemistry-Paraffin.

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. TRAC-1 (T-cell RING activation protein 1), also known as RNF125 (ring finger protein 125) or E3 ubiquitin-protein ligase RNF125, is a 232 amino acid novel E3 ubiquitin ligase that functions as a positive regulator in the T-cell receptor signaling pathway. Expressed predominantly in lymphoid tissues such as spleen, thymus and bone marrow, TRAC-1 has been found to inhibit pathogen-induced cytokine production and down-regulates HIV replication.

Supplier: Bioss

RNF41 contains one RING-type zinc finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. It acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins, such as ERBB3. RNF41 has been detected in ovary, testis and prostate.

Supplier: Bioss

E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone.

Supplier: Genetex

Rabbit Polyclonal antibody to GABRG2

Supplier: G-Biosciences

E3 Ubiquitin ligase inhibitor.

Supplier: Bioss

Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1.

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 UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells.

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). MARCH3 (membrane-associated ring finger (C3HC4) 3), also known as RNF173, is a 253 amino acid multi-pass membrane protein that localizes to cytoplasmic vesicles and early endosomes and contains one RING-CH-type zinc finger. Involved in the pathway of protein modification, MARCH3 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to be involved in endosomal trafficking 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). MARCH3 (membrane-associated ring finger (C3HC4) 3), also known as RNF173, is a 253 amino acid multi-pass membrane protein that localizes to cytoplasmic vesicles and early endosomes and contains one RING-CH-type zinc finger. Involved in the pathway of protein modification, MARCH3 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to be involved in endosomal trafficking events.

Supplier: Rockland Immunochemical

The Pellino proteins are a highly homologous family of E3 ubiquitin ligases that act as upstream mediators in Toll-like receptor (TLR) pathways that lead to activation of MAP kinases and transcription factors. Pellino 1 is required for interleukin-1-mediated signaling through its interaction with the IRAK4-IRAK-TRAF6 complex, ultimately resulting in the activation of NF-kB. Like other members of the Pellino family, Pellino 1 is an E3 ubiquitin ligase, able to catalyze the polyubiquitination of IRAK1. It is activated via phosphorylation by either IRAK1 and IRAK4 or the IKK-related kinases IKK-e and TBK1. In addition to phosphorylation, Pellino 1 activity is also modulated via ubiquitination and sumoylation.

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. TRAC-1 (T-cell RING activation protein 1), also known as RNF125 (ring finger protein 125) or E3 ubiquitin-protein ligase RNF125, is a 232 amino acid novel E3 ubiquitin ligase that functions as a positive regulator in the T-cell receptor signaling pathway. Expressed predominantly in lymphoid tissues such as spleen, thymus and bone marrow, TRAC-1 has been found to inhibit pathogen-induced cytokine production and down-regulates HIV replication.

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. TRAC-1 (T-cell RING activation protein 1), also known as RNF125 (ring finger protein 125) or E3 ubiquitin-protein ligase RNF125, is a 232 amino acid novel E3 ubiquitin ligase that functions as a positive regulator in the T-cell receptor signaling pathway. Expressed predominantly in lymphoid tissues such as spleen, thymus and bone marrow, TRAC-1 has been found to inhibit pathogen-induced cytokine production and down-regulates HIV replication.

Supplier: Bioss

Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis.

Supplier: Bioss

May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition.

Supplier: Bioss

May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition.

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

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: 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

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

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Novus Biologicals

The SARS2 Antibody from Novus Biologicals is a rabbit polyclonal antibody to SARS2. This antibody reacts with human. The SARS2 Antibody has been validated for the following applications: Immunohistochemistry, Immunohistochemistry-Paraffin.

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). MARCH3 (membrane-associated ring finger (C3HC4) 3), also known as RNF173, is a 253 amino acid multi-pass membrane protein that localizes to cytoplasmic vesicles and early endosomes and contains one RING-CH-type zinc finger. Involved in the pathway of protein modification, MARCH3 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to be involved in endosomal trafficking events.

Supplier: Bioss

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation.

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). MARCH3 (membrane-associated ring finger (C3HC4) 3), also known as RNF173, is a 253 amino acid multi-pass membrane protein that localizes to cytoplasmic vesicles and early endosomes and contains one RING-CH-type zinc finger. Involved in the pathway of protein modification, MARCH3 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to be involved in endosomal trafficking events.

Supplier: Bioss

Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis.

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

Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1.

Supplier: Bioss

DZIP3 is a 1,208 amino acid protein that localizes to the cytoplasm and contains one RING-type zinc finger. Expressed in a variety of tissues with highest expression in heart, skeletal muscle and kidney, DZIP3 functions as an E3 ubiquitin-protein ligase that accepts ubiquitin from an E2 ubiquitin-conjugating enzyme, thereby playing a role in signaling events throughout the cell. Multiple isoforms of DZIP3 exist due to alternative splicing events.

Supplier: Bioss

Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1.