622 Results for: "Biosensis"

Supplier: Biosensis

May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. Ref: uniprot.org.

Supplier: Biosensis

May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. Ref: uniprot.org

Supplier: Biosensis

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins (PubMed:10926528, PubMed:12044163, PubMed:11972040, PubMed:16908857, PubMed:16586416, PubMed:17060607, PubMed:17449675, PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341, PubMed:25205354, PubMed:27458239). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:1396673, PubMed:15111114). Ref: uniprot.org

Supplier: Biosensis

Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). Ref: uniprot.org

Supplier: Biosensis

The Biosensis NT3 Rapid™ enzyme-linked immune-sorbent assay (ELISA) kit is a sandwich ELISA that allows the specific, fast and reliable quantification of NT3 in less than 4 hours in cell culture supernatants and human plasma (EDTA and citrate) only if used as directed.

Supplier: Biosensis

Lipid phosphate phosphohydrolase 3 (LPP3) is a member of the phosphatidic acid phosphatase (PAP) family. LPP3 catalyzes the conversion of phosphatidic acid to diacylglycerol. In addition it hydrolyzes lysophosphatidic acid, ceramide-1-phosphate and sphingosine-1-phosphate (Ref: SWISSPROT).

Supplier: Biosensis

Galectin 3 is a lectin with carbohydrate recognition domains (CRD) which bind  -galactoside. It is a multifunctional protein expressed both on the cell surface, cytoplasm and nucleus and appears to have roles in specific carbohydrate binding and in the regulation of mRNA splicing.

Supplier: Biosensis

Myelin is a membrane characteristic of the nervous tissue and functions as an insulator to increase the velocity of the stimuli being transmitted between a nerve cell body and its target. Myelin isolated from human and bovine nervous tissue is composed of approximately 80% lipid and 20% protein, and 30% of the protein fraction constitutes myelin basic protein (MBP). MBP is an 'intrinsically unstructured' protein with a high proportion (approximately 75%) of random coil, but postulated to have core elements of beta-sheet and alpha-helix. MBP is a major protein in CNS myelin and is expressed specifically in the nervous system. A detailed immunochemical examination of monoclonal and polyclonal antibody responses to MBP and its peptides has revealed the existence of as many as 27 antigenic determinants, many of them conformational. Topological mapping of the potential antigenic determinants onto a model of MBP secondary structure places these determinants within 11 separate regions of the molecule, including those portions that have been found to be encephalitogenic. The message for myelin basic protein is selectively translocated to the ends of the cell processes. Immunization with myelin-associated antigens including MBP significantly promotes recovery after spinal cord contusion injury in the rat model. FUNCTION: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity). SUBUNIT: Homodimer (By similarity). SUBCELLULAR LOCATION: Myelin membrane; peripheral membrane protein; cytoplasmic side. Cytoplasmic side of myelin. TISSUE SPECIFICITY: Found in both the central and the peripheral nervous system.

Supplier: Biosensis

Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR) and upon binding to the receptor it induces the release of growth hormone from the pituitary. This ligand has an appetite-stimulating effect and is involved in growth regulation (Ref: SWISSPROT).

Supplier: Biosensis

Proopiomelanocortin (POMC) is the precursor of the melanocortin peptides alpha, beta and gamma. POMC neurons in the arcuate nucleus of the hypothalamus function as key central regulators of food intake and homeostatic control of energy balance in both rodents and non-human primates. MSH increases the pigmentation of skin by increasing the melanin production in melanocytes. MSH is produced in the pituitary gland and belongs to the POMC family.

Supplier: Biosensis

Microtubules are 25nm diameter protein rods found in most kinds of eukarytic cells. They are polymerized from a dimeric subunit made of one a subunit and one b tubulin subunit. Microtubules are associated with a family of proteins called microtubule associated proteins (MAPs), which includes the protein t (tau) and a group of proteins referred to as MAP1, MAP2, MAP3, MAP4 and MAP5. MAP2 is made up of two ~280kDa apparent molecular weight bands referred to as MAP2a and MAP2b. A third lower molecular weight form, usually called MAP2c, corresponds to a pair of protein bands running at ~70kDa on SDS-PAGE gels. All these MAP2 forms are derived from a single gene by alternate transcription, and all share a C-terminal sequence which includes either three or four microtubule binding peptide sequences, which are very similar to those found in the related microtubule binding protein t (tau). MAP2 isoforms are expressed only in neuronal cells and specifically in the perikarya and dendrites of these cells. Antibodies to MAP2 are therefore excellent markers on neuronal cells, their perikarya and neuronal dendrites.

Supplier: Biosensis

Alpha synuclein is an abundant 140 amino acid neuronal protein, expressed primarily at presynaptic terminals in the central nervous system. FUNCTION: May be involved in the regulation of dopamine release and transport. Soluble protein, normally localized primarily at the presynaptic region of axons, which can form filamentous aggregates that are the major non amyloid component of intracellular inclusions in several neurodegenerative diseases (synucleinopathies). Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase 3 activation. TISSUE SPECIFICITY: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.SUBUNIT: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1. Interacts with phospholipase D and histones. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Nucleus. Note=Membrane-bound in dopaminergic neurons. Also found in the nucleus. ALTERNATIVE PRODUCTS: 3 named isoforms produced by alternative splicing. Additional isoforms seem to exist.

Supplier: Biosensis

Obestatin is generated from the proteolytic cleavage of Ghrelin. Obestatin is a hormone that is produced in specialized epithelial cells of the stomach and small intestine of several mammals including humans.[2] Obestatin was originally identified as an anorectic peptide, but its effect on food intake remains controversial.

Supplier: Biosensis

Beta-adrenergic receptors are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family. Their function is to mediate the catecholamine-induced activation of adenylate cyclase through the action of G-proteins (ref: SWISSPROT).

Supplier: Biosensis

FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.  SUBCELLULAR LOCATION: Cytoplasm; cytosol. Cell membrane. Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. ALTERNATIVE PRODUCTS: 8 named isoforms produced by alternative splicing. Additional isoforms seem to exist. Isoforms differ from each other by the presence or absence of up to 5 of the 15 exons. One of these optional exons contains the additional tau/MAP repeat. TISSUE SPECIFICITY: Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system. DEVELOPMENTAL STAGE: Four-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain. DOMAIN: The tau/MAP repeat binds to tubulin. In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments  and straight filaments, mainly composed of hyperphosphorylated forms of Microtubule-associated protein Tau. Defects in Microtubule-associated protein Tau are a cause of frontotemporal dementia and parkinsonism linked to chromosome 17, as well as a number of other neurodegenerative diseases.

Supplier: Biosensis

FUNCTION: Involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1. SUBUNIT: Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-tubulin. Interacts with ULK1. SUBCELLULAR LOCATION: Golgi apparatus. TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. Expressed at very low levels in lung, thymus and small intestine. SIMILARITY: Belongs to the MAP1 LC3 family.

Supplier: Biosensis

Gamma synuclein belongs to the synuclein family which are believed to be involve in the pathogenesis of neurodegenerative diseases. High levels of gamma synuclein have been identified in andvanced breast carcinomas suggesting a correlation between gamma synuclein overexpression and breast tumor development. Gama synuclein plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway. SUBUNIT: May be a centrosome-associated protein. SUBCELLULAR LOCATION: Cytoplasm; perinuclear region. Centrosome. Spindle. Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle. TISSUE SPECIFICITY: Highly expressed in brain, particularly in the substantia nigra. Also expressed in the corpus callosum, heart, skeletal muscle, ovary, testis, colon and spleen. Weak expression in pancreas, kidney and lung. PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on residues distinct from the residue phosphorylated by other kinases. DISEASE: Brain iron accumulation type 1 (NBIA1, also called Hallervorden-Spatz syndrome), a rare neuroaxonal dystrophy, is histologically characterized by axonal spheroids, iron deposition, Lewy body (LB)-like intraneuronal inclusions, glial inclusions and neurofibrillary tangles. SNCG is found in spheroids but not in inclusions.

Supplier: Biosensis

Ubiquitin is a highly conserved 76 amino acid protein with an estimated molecular weight of 8.56 kDa which has a central role in regulated protein degradation. It is a protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Several types of polymeric chains can be formed depending on the lysine used for the assembly. Attachment to proteins as a polymer leads to their degradation by the 26S proteosome; a complex, multicatalytic cytosolic and nuclear protease. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous functions, including maintenance of chromatic structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair. Ubiquitin is synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats of which differ between species and strains. In some species there is a final amino-acid after the last repeat, here in bovine a Cys. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a).

Supplier: Biosensis

Beta-synuclein is a non-amyloid component of senile plaques found in Alzheimer disease. It could act as a regulator of SNCA aggregation. It protects neurons from staurosporine and 6 hydroxy dopamine -stimulated capspase activation in a p53-dependent manner. It localises to the cytoplasm and it is predominantly expressed in the brain where it is most concentrated in presynaptic nerve terminals. This protein is phosphorylated. This protein is also associated with the disease Brain iron accumulation type 1 (NBIA1).

Supplier: Biosensis

FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons. SUBUNIT: Homodimer, associated by noncovalent forces. SUBCELLULAR LOCATION: Secreted protein. SIMILARITY: Belongs to the NGF-beta family.

Supplier: Biosensis

The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.

Supplier: Biosensis

SOD3 is a member of the superoxide dismutase protein family. SODs are antioxidant enzymes that catalyse the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. SOD3 is thought to protect the brain, lungs and other tissues from oxidative stress. It is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A small percentage of SOD3 is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the extracellular matrix.

Supplier: Biosensis

CNTF is a survival promoting factor for different types of neurons in vitro and in vivo. The essential structural features for the biological function of human CNTF were investigated by Thier, M. et al. They showed that deletion of 14 N-terminal and 18 C-terminal amino acids significantly increased bioactivity compared to wild-type CNTF. FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Nervous system. PHARMACEUTICAL: CNTF is being tested under the name Axokine by Regeneron Pharmaceuticals for treatment of human motor neuron diseases, such as amyotrophic lateral sclerosis (ALS). As it induces substantial weight loss, preferentially of fat as opposed to lean body mass, it is being used for obesity treatment. SIMILARITY: Belongs to the CNTF family.

Supplier: Biosensis

FUNCTION: Seems to promotes the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family.

Supplier: Biosensis

FUNCTION: Can mediate activation of c-Jun and NF-kappa-B. May promote caspase-independent cell death. Isoform 2 and isoform 3 may act as decoy receptors. SUBUNIT: Associates with TRAF1, TRAF2, TRAF3 and TRAF5. SUBCELLULAR LOCATION: Isoform 1, isoform 3, isoform 4: Cell membrane; single-pass type I membrane protein (Probable). Isoform 2: Secreted protein (Probable). ALTERNATIVE PRODUCTS: 4 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Highly expressed in adult brain, and in embryos from day 11-17, but not earlier. Detected in embryonic brain and epithelium, and at lower levels in adult heart, lung and liver. In neonatal mice, mainly in hair follicles and neuron-like cells in the cerebellum, but not in the skin epidermis. Isoform 3 was found in embryonic day 17.5 skin but not in brain and liver. SIMILARITY: Contains 3 TNFR-Cys repeats.

Supplier: Biosensis

Myelin is a membrane characteristic of the nervous tissue and functions as an insulator to increase the velocity of the stimuli being transmitted between a nerve cell body and its target. Myelin isolated from human and bovine nervous tissue is composed of approximately 80% lipid and 20% protein, and 30% of the protein fraction constitutes myelin basic protein (MBP). MBP is an 'intrinsically unstructured' protein with a high proportion (approximately 75%) of random coil, but postulated to have core elements of beta-sheet and alpha-helix. MBP is a major protein in CNS myelin and is expressed specifically in the nervous system. A detailed immunochemical examination of monoclonal and polyclonal antibody responses to MBP and its peptides has revealed the existence of as many as 27 antigenic determinants, many of them conformational. Topological mapping of the potential antigenic determinants onto a model of MBP secondary structure places these determinants within 11 separate regions of the molecule, including those portions that have been found to be encephalitogenic. The message for myelin basic protein is selectively translocated to the ends of the cell processes. Immunization with myelin-associated antigens including MBP significantly promotes recovery after spinal cord contusion injury in the rat model. FUNCTION: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity). SUBUNIT: Homodimer (By similarity). SUBCELLULAR LOCATION: Myelin membrane; peripheral membrane protein; cytoplasmic side. Cytoplasmic side of myelin. TISSUE SPECIFICITY: Found in both the central and the peripheral nervous system. PTM: At least 5 charge isomers; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4 and C5 (the least cationic form); are produced as a result of optional posttranslational modifications such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. C1 and C2 are unphosphorylated, C3 and C4 are monophosphorylated and C5 is phosphorylated at two positions. SIMILARITY: Belongs to the myelin basic protein family.

Supplier: Biosensis

Fibroblast growth factors (FGFs), a heparin binding growth factor, exhibit widespread mitogenic and neurotrophic activities in a variety of different cells including mesenchymal, neuroectodermal and endothelial cells. aFGF (FGF-1) and bFGF (FGF-2) are present in relatively high levels in CNS. aFGF is expressed by a subset of neuronal populations, while bFGF is expressed by astrocytes, both lack signal peptides. Human bFGF is a 17.2 kDa protein containing 155 amino acid residues. FUNCTION: The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors. SUBUNIT: Monomer. Interacts with CSPG4 and FGFBP1. Found in a complex with FGFBP1, FGF1 and FGF2. MISCELLANEOUS: This protein binds heparin more strongly than does aFGF. SIMILARITY: Belongs to the heparin-binding growth factors family.

Supplier: Biosensis

GDNF is a glycosylated, disulfide-bonded homodimer molecule. It was first discovered as a potent survival factor for midbrain dopaminergic neurons and was then shown to rescue these neurons in animal models of Parkinson's disease. GDNF is about 100 times more efficient survival factor for spinal motor neurons than the neurotrophins. FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. DISEASE: Defects in GDNF may be a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, defects in GDNF may be involved in Hirschsprung disease. This genetic disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. DISEASE: Defects in GDNF are a cause of congenital central hypoventilation syndrome (CCHS); also known as congenital failure of autonomic control or Ondine curse. CCHS is a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.

Supplier: Biosensis

FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. PTM: The anchoring of this receptor to the plasma membrane is probably mediated by the palmitoylation of a cysteine residue. MISCELLANEOUS: The rank order of affinity of this receptor to tachykinins is: neuromedin K > substance K > substance P. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.

Supplier: Biosensis

FUNCTION: GABARAPL1 (GABARAPL2 or GABARAP or MAP1LC3)-modifier protein conjugating enzyme involved in its E2-like covalent binding to PE. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3 (E2-like enzyme). Preferred substrate is MAP1LC3A. Formation of the GABARAPL1-PE conjugate is essential for autophagy. SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta. SIMILARITY: Belongs to the ATG3 family.