"Biosensis"

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).

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Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC). Ref: uniprot.org

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Saporin is a ribosome-inactivating protein (RIP) of type I. This monomeric RNA N-glycosidase purified from seeds of the plant Saponaria officinalis also known as Soapwort, is capable of specific depurination of eukaryotic ribosomes thus arresting protein synthesis. No ligand has been identified in saporin hence its inability to transverse the cell membrane. Due to its toxicity and stability of the structure, saporin has proven extremely useful for construction of immunotoxins.

Supplier: Biosensis

BDNF belongs to the neurotrophin family and promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. It is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. Post translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family.

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

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

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 LR³IGF-I Rapid™ ELISA Kit consists of a complete set of reagents and pre-coated plate to allow immediate assay of LR³IGF-I in culture media. Included in the kit are mouse monoclonal anti- LR³IGF-I capture antibody pre-coated onto an ELISA plate, standard LR³IGF-I protein, a biotinylated anti- LR³IGF-I detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3’,5,5’-tetramethylbenzidine, TMB) yields a coloured reaction product which is directly proportional to the concentration of LR³IGF-I present in samples and the supplied protein standard.

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

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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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

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).

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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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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

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

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