44160 Results for: "Bioss"

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Leucine-rich protein (LRP130) is a cytoplasmic mRNA-binding protein likely to be involved in the processing of mitochondrial DNA transcripts. Defects in the LRPPRC gene that encodes LRP130 result in the French-Canadian type of Leigh syndrome, a severe neurological disorder characterized by lesions in the subcortical region of the brain. LRP130 also interacts with the low-affinity receptor for leukemia inhibitory factor to produce an intracelluar signal cascade.

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RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

Leucine-rich protein (LRP130) is a cytoplasmic mRNA-binding protein likely to be involved in the processing of mitochondrial DNA transcripts. Defects in the LRPPRC gene that encodes LRP130 result in the French-Canadian type of Leigh syndrome, a severe neurological disorder characterized by lesions in the subcortical region of the brain. LRP130 also interacts with the low-affinity receptor for leukemia inhibitory factor to produce an intracelluar signal cascade.

Supplier: Bioss

Leucine-rich protein (LRP130) is a cytoplasmic mRNA-binding protein likely to be involved in the processing of mitochondrial DNA transcripts. Defects in the LRPPRC gene that encodes LRP130 result in the French-Canadian type of Leigh syndrome, a severe neurological disorder characterized by lesions in the subcortical region of the brain. LRP130 also interacts with the low-affinity receptor for leukemia inhibitory factor to produce an intracelluar signal cascade.

Supplier: Bioss

HN1L

Supplier: Bioss

Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine.

Supplier: Bioss

Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).

Supplier: Bioss

Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).

Supplier: Bioss

Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).

Supplier: Bioss

IGSF21 is a 467 amino acid secreted protein that contains two Ig-like (immunoglobulin-like) domains and is a member of the immunoglobulin superfamily. Members of this family of proteins usually localize to the cell membrane, and may act as receptors in the immune response pathways. The gene encoding IGSF21 maps to human chromosome 1p36.13 and mouse chromosome 4 D3. Human chromosome 1 spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome. A large number of disease-associated genes are associated with chromosome 1, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome. Aberrations in chromosome 1 are found in a variety of cancers, including head and neck cancer, malignant melanoma and multiple myeloma.

Supplier: Bioss

E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Supplier: Bioss

E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Supplier: Bioss

E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Supplier: Bioss

E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

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. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

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). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.

Supplier: Bioss

Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.

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. ZDHHC1 (zinc finger, DHHC-type containing 1), also known as ZNF377 (zinc finger protein 377) or C16orf1, is a 485 amino acid multi-pass membrane protein that contains one DHHC-type zinc finger. Expressed in fetal heart, lung and kidney and also present in adult lung and pancreas, ZDHHC1 functions as a palmitoyltransferase that catalyzes the conversion of palmitoyl-CoA and protein-cysteine to S-palmitoyl protein and CoA. Like ZDHHC1, ZDHHC5, ZDHHC6, ZDHHC7 and ZDHHC18 each contain one DHHC-type zinc finger through which they convey palmitoyltransferase activity against a broad range of substrates, including H-Ras, SNAP 25 and GABAA R proteins.

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. ZDHHC1 (zinc finger, DHHC-type containing 1), also known as ZNF377 (zinc finger protein 377) or C16orf1, is a 485 amino acid multi-pass membrane protein that contains one DHHC-type zinc finger. Expressed in fetal heart, lung and kidney and also present in adult lung and pancreas, ZDHHC1 functions as a palmitoyltransferase that catalyzes the conversion of palmitoyl-CoA and protein-cysteine to S-palmitoyl protein and CoA. Like ZDHHC1, ZDHHC5, ZDHHC6, ZDHHC7 and ZDHHC18 each contain one DHHC-type zinc finger through which they convey palmitoyltransferase activity against a broad range of substrates, including H-Ras, SNAP 25 and GABAA R proteins.

Supplier: Bioss

Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity.

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Mono-ADP-ribosylation is one of the posttranslational protein modifications regulating cellular metabolism (e.g. nitrogen fixation) in prokaryotes. Mono-ADP-ribosylation is a process in which the ADP-ribose moiety of nicotinamide adenine dinucleotide is transferred to an acceptor amino acid. Five mammalian ADP-ribosyltransferases (ART1-ART5) have been cloned, and each ART is expressed in different tissues. ART5 (ADP-ribosyltransferase 5), also known as Ecto-ADP-ribosyltransferase 5, is a 292 amino acid secretory protein that is expressed in testis, heart, skeletal muscle and lymphoma. Functionally, ART5 is implicatetd to play a role in cell signaling and metabolism cascades. Two isoforms of ART5 exist as a result of alternative splicing events.

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Glutathione (GSH) is a tripeptide antioxidant that reduces disulfide bonds between cytoplasmic proteins. The constitutive enzyme glutathione reductase transforms glutathione into its reduced state, which ultimately can provide a measure of cellular toxicity. GSTCD (glutathione S-transferase, C-terminal domain containing) is a 633 amino acid protein belonging to the GSTCD family and contains one GST C-terminal domain. The gene encoding GSTCD maps to human chromosome 4, which represents approximately 6% of the human genome and contains nearly 900 genes. Notably, the Huntingtin gene, which is found to encode an expanded glutamine tract in cases of Huntington's disease, is on chromosome 4. FGFR-3 is also encoded on chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease.

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Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle, that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein), also designated MEN, functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. It is also thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, with lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary. ELL3 is a 397 amino acid nuclear protein that functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. Though similar to ELL and ELL2, ELL3 is exclusively expressed in testis.

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Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Appears be required for postnatal control of vascular regression in the eye. Required for posterior patterning of the epiblast during gastrulation.

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G-protein coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD) (PubMed:28129538). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors (PubMed:28129538). Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways (PubMed:28129538). Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca2+ ions from intracellular stores (PubMed:18703043, PubMed:28129538). Affects neural activity, perception, cognition and mood (PubMed:18297054). Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction.

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Osteopontin is the principal phosphorylated glycoprotein of bone and is expressed in a limited number of other tissues including dentine. Osteopontin is produced by osteoblasts under stimulation by calcitriol and binds tightly to hydroxyapatite. It is also involved in the anchoring of osteoclasts to the mineral of bone matrix via the vitronectin receptor, which has specificity for osteopontin. Osteopontin is overexpressed in a variety of cancers, including lung, breast, colorectal, stomach, ovarian, melanoma and mesothelioma.

Supplier: Bioss

CBP tag is a calmodulin-binding peptide, KRRWKKNFIAVSAANRFKKISSSGAL, derived from skeletal/cardiac muscle myosin light chain kinase 2.

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Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival. (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:9427609, PubMed:10074122, PubMed:10756055). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205).

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Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization.