622 Results for: "Biosensis"

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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.

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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.

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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.

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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

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

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.

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Tyrosine hydroxylase is an excellent marker for dopaminergic and noradrenergic neurons. Tyrosine hydroxylase (a.k.a. tyrosine 3-monooxygenase) is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). L-DOPA is a precursor for dopamine, which, in turn, is a precursor for the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline). Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines. In humans, tyrosine hydroxylase is encoded by the TH gene, and the enzyme is present in the central nervous system (CNS), peripheral symphatic neurons and the adrenal medulla. The enzymatic activity of TH requires ferrous ions as cofactors and is believed to be regulated by phosphorylation. At least four isoforms of human TH have been identified which result from alternative splicing. Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs). http://en.wikipedia.org/wiki/Tyrosine_hydroxylase

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Adenylate cyclases are enzymes which interact with and are activated by the GTP bound alpha subunits of trimeric G-proteins. Activated adenylate cyclases are responsible for the production of the important "second messenger" signalling molecule cyclic-AMP, which is generated from ATP. The type III adenylate cyclase enzyme is localized in the membranes surrounding the cilia in neurons, and our antibody is an excellent marker of neuronal cilia in the brain and in cells in tissue culture. Adenylate cyclase type III is a large complex molecule of, in the human, 1145 amino acids with a deduced molecular weight of 129kDa. The protein may be variably glycosylated, so that on SDS-PAGE and western blots it runs as a diffuse band of about 160kDa in cortex and about 200kDa in olfactory epithelium. The molecule has a complex structure, with 12 transmembrane domains and two cyclase domains. Each cyclase domain is immediately C-terminal to 6 transmembrane segments, but only the second, C-terminal cyclase is believed to be catalytically active.

Supplier: Biosensis

Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface (PubMed:27362226). Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization (PubMed:24867636). It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed (Probable). Ref: uniprot.org

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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

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

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.

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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

The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

Supplier: Biosensis

FUNCTION: Functions as an E1 enzyme essential for multisubstrates such as GABARAPL1 and ATG12. Forms intermediate conjugates with GABARAPL1 (GABARAPL2, GABARAP or MAP1ALC3). Formation of the final GABARAPL1-PE conjugate is essential for autophagy. SUBUNIT: Homodimer (By similarity). Interacts with ATG3 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. SUBCELLULAR LOCATION: Cytoplasm (Probable). ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. DOMAIN: The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12. SIMILARITY: Belongs to the ATG7 family. In yeast, ATG7 appears to be required for fusion of peroxisomal and vaculuolar membranes.

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

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

The Biosensis GDNF RapidTM enzyme-linked immunosorbent assay (ELISA) Kit is a sandwich ELISA that allows the quantification of GDNF in less than 4 hours in cell culture supernatants, cell lysates, and serum only if used as directed. Please refer to the kit protocol for specific use instructions for each substrate application, in particular mouse serum samples.

Supplier: Biosensis

The Biosensis Multi-Neurotrophin Rapid™ Screening ELISA Kit has been designed to allow rapid screening and quantification of NGF, BDNF, NT3 and NT4/5 in cell culture supernatants, lysates, serum, plasma (EDTA and citrate) and brain extracts only if used as directed.

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.

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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.

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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.

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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).

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Nestin is a member of the class IV intermediate filament protein family which is expressed in neuronal stem cells. The molecular weight of human Nestin as determined by SDS-PAGE mobility is about 240kDa. However the real molecular weight is considerably less than this, at 177kDa, the disparity being likely due to the highly charged region of the C-terminal segment. Nestin is relatively poorly conserved in protein sequence across species boundaries, so that the mouse and human proteins have an overall identity of only 62%. As a result antibodies to the human protein often fail to recognize the rodent homologue and vice versa. However this antibody stains both rodent and human Nestin. Antibodies to Nestin are widely used to identify neural stem cells.

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Neuropeptide VF is the precursor of neuropeptides NPSF (RFRP-1), RFRP-2 and RFRP-3 (NPVF). RFRP-3 is reported to inhibit forskolin-induced production of cAMP. RFRP-3 has also been shown to block morphine-induced analgesia.

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.