622 Results for: "Biosensis"

Supplier: Biosensis

The causes and effects of neuronal degeneration are of major interest to a wide variety of neuroscientists. Paralleling this growing interest is an increasing number of methods applicable to the detection of neuronal degeneration. The fluorescent dye Fluoro-Jade® B (FJB), like its more purified brother Fluoro-Jade® C (FJC), is an anionic fluorescein derivative useful for the histological staining of neurons undergoing degeneration.

Supplier: Biosensis

Anti-LMNA Mouse T4 Antibody [clone: 4C4]

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Anti-ACTA Mouse T4 Antibody [clone: 5J11]

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Anti-TNR16 Mouse Monoclonal Antibody [clone: Clone: Me20.4] (Atto 488)

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Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake (Ref: uniprot.org). ProGDNF is the unprocessed precursor molecule of mature GDNF and exists as homodimer.

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Amylo-Glo RTD reagent is designed to stain amyloid plaques in tissue sections.

Supplier: Biosensis

GAP43 is very abundant protein which is found concentrated in neurons. One group discovered it as one of three proteins which becomes unregulated during the regeneration of the toad optic nerve (1). Three GAPs (Growth associated proteins) were discovered, and the number 43 comes from the apparent SDS-PAGE molecular weight of the one named GAP43. The HGNC name for this protein is, not surprisingly, GAP43. Later work showed that GAP43 does not run on SDS-PAGE in a fashion which accurately reflects its molecular weight, and that GAP43 proteins from different species may run at different apparent molecular weights. Partly due to these features GAP43 were independently discovered by several different groups and therefore has several alternate names, such as protein F1, pp46, neuromodulin, neural phosphoprotein B-50 and calmodulin-binding protein P-57. In each case the number reflects the apparent SDS-PAGE molecular weight, and underlines the unusual properties of this molecule. Mammalian GAP43 proteins contains only 226-243 amino acids, and so the real molecular weight is 23.61-25.14 kDa. GAP43 has been extensively studied and is known to be a major protein kinase C substrate and to bind calmodulin avidly. GAP43 is anchored to the plasma membrane by palmitoylation modifications.

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Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels. MMP2 isoform 2 mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways. Catalytic activity of MMP2 causes cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. (Ref: uniprot.org).

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 spectrin family of proteins were originally discovered as major components of the submembraneous cytoskeleton of osmotically lysed red blood cells (1). The lysed blood cells could be seen as clear red blood cell shaped objects in the light microscope and were referred to as red cell "ghosts". The major proteins of these ghosts proved to be actin, ankyrin, band 4.1 and several other proteins, including two major bands running at about 240kDa and 260kDa on SDS-PAGE gels. This pair of bands was named "spectrin" since they were discovered in these red blood cell ghosts (1). Later work showed that similar high molecular bands were seen in membrane preparations from other eukaryotic cell types. Work by Levine and Willard described a pair of about ~240-260kDa molecular weight bands which were transported at the slowest rate along mammalian axons (2). They named these proteins "fodrin" as antibody studies showed that they were localized in the sheath under the axonal membrane, but not in the core of the axon (2; fodros is Greek for sheath). Subsequently fodrin was found to be a member of the spectrin family of proteins, and the spectrin nomenclature is now normally used (3). Spectrins form tetramers of two alpha and two beta subunits, with the alpha corresponding to the lower molecular weight ~240kDa band and the beta corresponding to the ~260kDa or in some case much larger band. Most spectrin tetramers are about 0.2microns or 200nm long, and each alpha and beta subunit has a cell type specific expression pattern. The basic structure of each spectrin subunit is the spectrin repeat, which is a sequence of about 110 amino acids which defines a compact domain contain three closely packed alpha-helices. Each spectrin subunit contains multiple copies of this repeat, with 20 in each of the alpha subunits. The beta I-IV subunits each contain 17 spectrin repeats, while the beta V subunit, also known as beta-heavy spectrin, contains 30 of these repeats. The various subunits also contain several other kinds of functional domain, allowing the spectrin tetramer to interact with a variety of protein, ionic and lipid targets. The alpha-subunits each contain one calmodulin like calcium binding region and one Src-homology 3 (SH3) domain, an abundant domain involved in specific protein-protein interactions. The beta subunits all have a N-terminal actin binding domain and may also have one SH3 domain and one pleckstrin homology domain, a multifunctional type of binding domain which in beta I spectrin at least binds the membrane lipid PIP2 (5). Spectrins are believed to have a function in giving mechanical strength to the plasma membrane since the tetramers associate with each other to form a dense submembraneous geodesic meshwork (3). They also bind a variety of other membrane proteins and membrane lipids, and the proteins they bind to are therefore themselves localized in the membrane. Diseases may be associated with defects in one or other of the spectrin subunits (6). For example, some forms of hereditary spherocytosis, the presence of spherical red blood cells which are prone to lysis, can be traced to mutations in some of the spectrin subunits (7). The alpha-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons. The antibody can therefore be used to identify neurons and fragments derived from neuronal membranes in cells in tissue culture and in sectioned material.

Supplier: Biosensis

The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (Aβ) associated with the pathology characteristic of Alzheimer’s disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for Aβ have been shown to actually detect intraneuronal APP and not Aβ exclusively.

MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to Aβ residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide. MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice).

Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for Aβ40 and Aβ42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10. In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal Aβ, distinct from Aβ associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.

Biosensis now offers biotinylated MOAB-2 antibody allowing more flexibility in experimental design by using the biotin-avidin/streptavidin detection method. Biotinylated MOAB-2 antibody may also help to reduce background staining in difficult-to-stain tissues and increase detection sensitivity. The ability of biotinylated MOAB-2 antibody to detect amyloid beta has been validated by IHC.

Supplier: Biosensis

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ref: uniprot.org. This antibody recognizes laminin isotypes alpha-1 (440 kDa), beta-1 (220 kDa) and gamma-1 (220 kDa). It also binds laminin binding protein at 120 kDa which always co-expresses with laminin.

Supplier: Biosensis

NGF receptor antibody clone 8J2 was developed specifically as a replacement for clone MLR2, which is no longer available anywhere for commercial use. Antibody reactivity for clone 8J2 has been validated for human, mouse and rat extracellular domain of p75NTR. Clone 8J2 has been demonstrated to perform equivalent to or better than MLR2 antibody in all testing.

Supplier: Biosensis

Sheep serum from non-immunised animals was purified by protein G affinity chromatography. This sheep IgG fraction can be used as negative control antibody for various immunological techniques where sheep primary antibodies are used.

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

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Calretinin is a calcium-binding protein which is abundant in auditory neurons. Ref: uniprot.org. Antibody is specific for calretinin and does not recognize closely related proteins parvalbumin and calbindin as determined by Western Blotting.

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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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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 protein named TrkB (also named Neurotrophic tyrosine kinase receptor type 2 (NTRK2), GP145-TrkB or Tropomyosin-related kinase B is a receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems and is important in the regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. TrkB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. TrkB is the primary receptor for BDNF (brain-derived neurotrophic factor. TrkB also binds NT4 and NT3 but less efficiently. (Reference: www.uniprot.org).

Applications: Flow Cytometry (5-10 ug/mL): Tested on human and rodent cell lines. Cell staining can be performed under native conditions on ice, or on fixed cells with up to 4% formaldehyde. Other applications have not been tested. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.

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Anti-PRPH Mouse Monoclonal Antibody [clone: 7C5]

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Mouse NGF (2.5S) was isolated from mouse submaxillary glands by method of Mobley et al (1976) and is a form of beta-NGF that has identical biological properties. NGF is known to regulate the survival and development of certain sympathetic and sensory neurons. It is a dimer with 2 identical polypeptide chains and dimeric molecular weight of approximately 26,500 Da. Isolation and purification of NGF from mouse submaxillary glands yields preparations of NGF (2.5S) with identical biological activity but with cleavages at the amino terminus (with the loss of 8 amino acids) and/or at the carboxy-terminus (with the loss of arginine). These preparations are named 2.5 NGF.

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Monoclonal antibody MC192 against the rat low affinity nerve growth factor receptor (p75NTR) is derived from the fusion of Sp2/0-Ag 14 myeloma cells with mouse immune splenocytes. MC192 monoclonal antibody was originally generated by Chandlers et al. p75NTR was originally discovered as a low affinity nerve growth factor receptor. Later it was found that it was the receptor for all neurotrophins. It mediates signals of neurotrophins for neuronal survival, apoptosis, neurite outgrowth and synaptic plasticity. Recently, it has been revealed that p75NTR not only acts as the receptor for neurotrophins but also the receptor for many other pathological ligands such as prions, rabies virus and amyloid beta. p75NTR also acts as a co-receptor for NOGO which mediates inhibitory signals of myelin associated protein. p75NTR is highly expressed in a number of non-neuronal and neuronal cells including motor neurons during development and also in damaged neurons. MC192 has a potential use as the ligand for gene delivery into p75NTR-expressing rat cells via a receptor-mediated mechanism.
This antibody reacts with rat only. Does not react with mouse or human NGFR

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SOD1 binds copper and zinc ions ans is one of two isozymes responsible for destroying free superoxide radicals which are normally produced within the cells and which are toxic to biological systems. SOD1 is a soluble cytoplasmic protein, acting as a homodimer to convert superoxide radicals to molecular oxygen and hydrogen peroxide. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) which is a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis.

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Beta-synuclein is a soluble cytoplasmic protein associated with synaptic vesicles and a member of the synuclein family. Mutations in alpha-synuclein cause early onset Parkinson's disease. Expression of beta synuclein may modulate alpha-synuclein aggregation found in Parkinson's disease.

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This gene encodes an enzyme which catalyzes the biosynthesis of the neurotransmitter acetylcholine. This gene product is a characteristic feature of cholinergic neurons, and changes in these neurons may explain some of the symptoms of Alzheimer's disease. Polymorphisms in this gene have been associated with Alzheimer's disease and mild cognitive impairment. Mutations in this gene are associated with congenital myasthenic syndrome associated with episodic apnea. Multiple transcript variants encoding different isoforms have been found for this gene, and some of these variants have been shown to encode more than one isoform. [provided by RefSeq, May 2010]

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Vimentin is the major protein subunit of the 10nm or intermediate filaments protein found in many kinds of mesenchymal and epithelia cells. Vimentin is also found in many kinds of cells in tissue culture and in developing neuronal and astrocytic precursor cells in the central nervous system. Vimentin frequently forms copolymers with other intermediate filament proteins, such as GFAP (in many kinds of astrocytes), with desmin (in muscle cells) and neurofilament proteins (in developing neurons). Antibodies to vimentin are useful in studies of stem cells and generally to reveal the filamentous cytoskeleton.

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Presenilin-1 (PSEN1) is a multi-pass membrane protein and component of the gamma-secretase complex. PSEN1 is thought to play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. It may also play a role in hematopoiesis. Defects in PSEN1 are a cause of Alzheimer disease type 3 (AD3), a familial early-onset form of Alzheimer disease (Ref:SWISS-Prot).

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TrkC is a member of the neurotrophic tyrosine receptor kinase family. TrkC is a membrane-bound receptor that upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. TrkC is the receptor for neurotrophin-3 (NT-3).  Signalling through TrkC leads to cell differentiation and may play a role in the development of proprioceptive neurons that sense body position. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. ALTERNATIVE PRODUCTS: 4 named isoforms produced by alternative splicing. Additional isoforms seem to exist. Mutations in TrkC have been associated with medulloblastomas, secretory breast carcinomas and other cancers.

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Peroxiredoxin-3 has a role in redox regulation of the cell.

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Lysine acetylation of histones and non-histone proteins plays an important part in many cellular processes such as chromatin and nuclear signaling, transcription, gene silencing, cell cycle progression, apoptosis, differentiation, DNA replication and repair.