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Fluoro-Jade stain is a fluorochrome derived from fluorescein, and is commonly used in neuroscience disciplines to label degenerating neurons in ex vivo tissue of the central nervous system.

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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).

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NT3 is a member of the neurotrophin family, that controls survival and differentiation of visceral and proprioceptive sensory neurons. NT3 is closely related to both NGF and BDNF. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NT3-deficient mice generated by gene targeting display sevvere movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family

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Hormone Sensitive Lipase (HSL) hydrolyzes stored triglycerides to free fatty acids in adipose tissue and heart. In steroidogenic tissues, HSL principally converts cholesteryl esters to free cholesterol for steroid hormone production (ref: SWISSPROT).

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C-reactive protein has several roles associated with host defence such as; promoting agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. It can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. COFACTOR: Binds 2 calcium ions per subunit. C-reactive protein exists as a homopentamer. There are 2 alternatively spliced isoforms. C-reactive protein is found in plasma and its concentration increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli. It is induced by IL-1 and IL-6.

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Neurofilaments are composed of three intermediate filament proteins: light (~68 kDa), medium (~160 kDa) and heavy (~200 kDa), which are involved in the maintenance of the neuronal caliber. Neurofilament medium runs on SDS-PAGE gels in the range 145-170 kDa, with some variation in different species.

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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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The Nuclear Core Complex (NPC) acts as a gateway for macromolecular traffic between the cytoplasm and the nucleus.

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DBH is an oxireductase belonging to the copper type II ascorbate-dependent monooxygenase family. DBH exists as a homotetramer composed of two non-covalently bound disulfide-linked dimers. It is present in the synaptic vesicles of postganglionic sympathetic neurons and converts dopamine to norepinephrine. It binds 2 copper ions and 1 PQQ per subunit . Depending on the presence of a signal peptide, DBH can exist in both soluble and membrane-bound forms.

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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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Human beta-endorphin is a 31 amino acid peptide cleaved from the precursor pro-opiomelanocortin (POMC). It is an endogenous opioid peptide neurotransmitter that interacts with opioid receptors.

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LRRK2 is a member of the leucine-rich repeat kinase family. Its role is yet unknown but it may play a role in the phoshorylation of proteins central to parkinson diseases. LRRK2 contains an ankryin repeat region, a leucine-rich repeat (LRR) domain, a kinase domain, a DFG-like motif, a RAS domain, a GTPase domain, a MLK-like domain and a WD40 domain. LRRK2 is present in the cytoplasm but also associates with the mitochondrial outer membrane. Defects in LRRK2 are the cause of Parkinson disease 8 (PARK8). Parkinson disease is characterised by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK8 is an autosomal-dominant late-onset parkinsonism, characterized by onset from 50 to 65 years, with slow progression and relatively benign course.

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The Human influenza hemagglutin (HA) tag corresponds to a region (98-106 amino acids) from the HA molecule.

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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

Catenin beta is an adherens junction protein and has a role in the regulation of cell adhesion and in signal transduction through the Wnt pathway. At least 2 isoforms are produced by alternative splicing.

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SUMO-1 binds to a wide range of target proteins as part of a post-translational modification system. Unlike ubiquitin, it does not seem to target protein for degradation, but is involved in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis, apoptosis, protein stability and signal transduction. SUBUNIT: Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. SUBCELLULAR LOCATION: Nucleus; nuclear membrane. Nucleus; nucleoplasm; nuclear speckle. Cytoplasm. SIMILARITY: Belongs to the ubiquitin family. SMT3 subfamily. SIMILARITY: Contains 1 ubiquitin-like domain. PTM: Cleavage of the last four amino acids of the carboxy-terminus of the precursor form by SENP1 or SENP2 is necessary for function. Several pseudogenes have been reported as well as a number of alternatively spliced isoforms.

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FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. SUBUNIT: Heterodimer. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with MAFB. SUBCELLULAR LOCATION: Nucleus. INDUCTION: C-fos expression increases upon a variety of stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, stress and cell injury. SIMILARITY: Belongs to the bZIP family. Fos subfamily. SIMILARITY: Contains 1 bZIP domain

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Peroxiredoxin-4 has a probable role in redox regulation of the cell.

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Nicastrin, a type 1 membrane glycoprotein, is an essential component of the gamma secretase complex which is critical for the cleavage of the amyloid precursor protein and other membrane proteins. Nicastrin is widely expressed in different tissue types. This antibody detects all processed forms of Nicastrin.

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Autosomal recessive mutations in DJ-1 cause early-onset familial Parkinson's disease. DJ-1 is considered a redox-sensitive cytoplasmic protein found in brain as well as other cell types.

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Histone H3 is a core component of nucleosome.

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Human Gastrin is a 101 amino acid hormone produced by G cells of the duodenum, stomach and pancreas. It stimulates secretion of hydrochloric acid by parietal cells of the stomach. Gastrin is also secreted into bloodstream.

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Autosomal dominant mutations in presenilin 2 are the second major cause of early-onset familial Alzheimer's disease. Presenilin 2 is a multi-transmembrane protein which undergoes endoprotelysis to form an N-terminal fragment of about 29 kDa and C-terminal fragment of about 22 kDa. Presenilin 2 forms the catalytic core of the gamma-secretase complex which cleaves type 1 transmembrane proteins including the amyloid precursor protein to generate the C-terminus of the amyloid beta peptide.

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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).

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Presenilin-2 (PSEN2) is a multi-pass membrane protein and component of the gamma-secretase complex. Defects in PSEN2 are a cause of Alzheimer disease type 4 (AD4), an autosomal dominant Alzheimer disease. (Ref:SWISS-Prot).

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NT3 is a member of the neurotrophin family, that controls survival and differentiation of visceral and proprioceptive sensory neurons. NT3 is closely related to both NGF and BDNF. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NT3-deficient mice generated by gene targeting display sevvere movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family.

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Alpha synuclein is an abundant 140 amino acid neuronal protein, expressed primarily at presynaptic terminals in the central nervous system. Alpha synuclein has been associated with several neurodegenerative diseases. A point mutation in the gene coding for the alpha-synuclein protein was the first discovery linking this protein to a rare familial form of Parkinson's disease (PD). Subsequently, other mutations in the alpha-synuclein gene have been identified in familial PD. The aggregated proteinaceous inclusions called Lewy bodies found in PD and cortical Lewy body dementia (LBD) were discovered to be predominantly alpha-synuclein. Aberrant aggregation of alpha-synuclein has been detected in an increasing number of neurodegenerative diseases, collectively known as synucleopathies. Alpha-synuclein exists physiologically in both soluble and membrane-bound states, in unstructured and alpha-helical conformations, respectively. The physiological function of alpha-synuclein appears to require its translocation between these subcellular compartments and interconversion between the 2 conformations. Abnormal processing of alpha-synuclein is predicted to lead to pathological changes in its binding properties and function.

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Neurofilaments contain three intermediate filament proteins: light (68 kDa), medium (160 kDa) and heavy (200 kDa). Neurofilament heavy (NF200 or NF-H) is phosphorylated and it is thought that this results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.

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FUNCTION: Required for autophagy. SUBUNIT: Conjugated to ATG5. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. SIMILARITY: Belongs to the ATG12 family.