622 Results for: "Biosensis"

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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mCherry is an engineered derivative of one of a family of proteins originally isolated from Cnidarians (jelly fish, sea anemones and corals). The mCherry protein was derived from DsRed, a red fluorescent protein from so-called disc corals of the genus Discosoma. DsRed is a 223 amino acid ~28kDa protein similar in size and properties to GFP, but, obviously, produces a red rather than a green fluorochrome. The original DsRed was engineered extensively in the Tsien lab to prevent it from forming tetramers and dimers and to modify and improve the spectral properties (1-3). The resulting monomeric protein is useful for applications such as Förster Resonance Energy Transfer (FRET, also known as Fluorescence Resonance Energy Transfer). Several further cycles of mutation, directed modification and evolutionary selection produced mCherry, which is monomeric and has an excitation maximum at 587 nm and and emission maximum at 610 nm (4).

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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.

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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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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.

Supplier: Biosensis

Black-Gold II is a novel haloaurophosphate complex which localises myelin within the central nervous system. The Black Gold II Ready-to-Dilute (RTD) Staining Kit allows you to localise myelin, both individual fibres and tracts, along with the option of co-localising cell bodies via the Toluidine Blue counter stain. Black Gold II labelled myelinated fibres appear nearly black while the Toluidine Blue O labelled cellular Nissl bodies are blue under bright field illumination.

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Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (PubMed: 8003967, PubMed: 25205354). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (By similarity). Ref: uniprot.org. Antibody detects arrestin-1 protein only and does not cross-react with the other 3 arrestin molecules.

Supplier: Biosensis

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

Supplier: Biosensis

Visinin (sometimes known as hippocalcin-like protein 3, HLP3, HPCAL3, HUVISL1, VLP-1, VILIP and VILIP-1) was originally isolated biochemically from chicken retina as a major protein of about 24kDa on SDS-PAGE. Following cloning and sequencing of visinin, several visinin like proteins were discovered by homology screening. One of these, Visinin-like protein 1 is a small Calcium binding protein which is very abundant in the nervous system and is found only in neurons, though different neurons have different levels of expression. It is particularly concentrated in cerebellar Purkinje cells, and tends to be most abundant in perikarya and dendrites. The protein belongs to the large superfamly of calmodulin and paravalbumin type proteins which function by binding Calcium ions. Calcium binding alters the confomation of these proteins and allow them to interact with other binding partners, the properties of which they may alter. Visinin-like protein 1 has four 'EF hand' domains, which are negatively charged helix-turn-helix peptides which are responsible for Calcium binding. Visinin-like protein 1 is 191 amino acids in size and has a molecular weight on SDS-PAGE of 22kDa.

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Anti-GFAP Mouse T4 Antibody [clone: 2A5]

Supplier: Biosensis

TrkA is a member of the neurotrophic tyrosine kinase receptor family. It is a membrane-bound receptor that upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. TrkA is required for high-affinity binding to nerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). TrkA leads to cell differentiations and may play a role in specifying sensory neuron subtypes. It has a crucial role in the development and function of the nociceptive reception system as well as establishment of thermal regulation via sweating. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. SUBCELLULAR LOCATION: Cell membrane; single-pass type I membrane protein. Endocytosed to the endosomes upon treatment of cells with NGF. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. Both isoforms have similar biological properties. TISSUE SPECIFICITY: Isoform TrkA-II is primarily expressed in neuronal cells. Isoform TrkA-I is found in non-neuronal tissues. Mutations in TrkA have been associated with congenital insensitivity to pain, anhidrosis, self-mutalating behaviour, mental retardation and cancer (Reference: www.uniprot.com).

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Rabbit anti-neuronal nuclei antigen/Fox3 (NeuN/Fox3) polyclonal antibody (unconjugated), suitable for WB, IHC, ICC.

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. Fluoro-Jade C stains all degenerating neurons regardless of specific insult or mechanism of cell death. Fluoro-Jade C exhibits the greatest signal to background ratio, as well as the highest resolution. This translates to a stain of maximal contrast and affinity for degenerating neurons. This makes it ideal for localising not only degenerating nerve cell bodies but also distal dendrites, axons and terminals. The dye is highly resistant to fading and is compatible with virtually all histological processing and staining protocols.

Supplier: Biosensis

FUNCTION: Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. ENZYME REGULATION: Inhibited by N-ethylmaleimide. SUBCELLULAR LOCATION: Cytoplasm (Probable).  SIMILARITY: Belongs to the peptidase C54 family.

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FUNCTION: Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. ENZYME REGULATION: Inhibited by N-ethylmaleimide. SUBCELLULAR LOCATION: Cytoplasm (Probable). ALTERNATIVE PRODUCTS: 5 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Mainly expressed in the skeletal muscle, followed by brain, heart, liver and pancreas. SIMILARITY: Belongs to the peptidase C54 family.

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FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. SUBUNIT: Interacts with LPL and SLC2A4. Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, GM2A and PSAP. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF). SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin. TISSUE SPECIFICITY: Expressed at high levels in brain, spinal cord, heart, skeletal muscle, thyroid, placenta and testis. Expressed at lower levels in lymphoid organs, kidney, colon and liver. INDUCTION: During osteoblast differentiation. DOMAIN: The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding. DOMAIN: The extracellular domain may be shed following protease cleavage in some cell types. PTM: The N-terminal propeptide is cleaved by furin and possibly other homologous proteases. PTM: Contains 8 intrachain disulfide bonds. PTM: N-glycosylated. SIMILARITY: Contains 9 BNR repeats.

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Neurotensin is a neuropeptide which regulates secretion of luteinizing hormone and prolactin. Involved in dopamine neurotransmission.

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.

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Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans Golgi network to lysosomes.  Together with medium and small subunits, adaptins form a heterotetrameric complex called an adaptor whose role is to promote the formation of clathrin-coated pits and vesicles and to recognise sorting signals within the cytosolic tails of transmembrane cargo molecules. Gamma-adaptin protein belongs to the adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network and/or endosomes. SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane.

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The Biosensis NGF Rapid™ enzyme-linked immunosorbent assay (ELISA) kit is a sandwich ELISA that allows the quantification of human NGF in less than 3 hours in cell culture supernatants, serum, plasma (citrate) and brain extracts only if used as directed.

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Peptide YY (PYY) is secreted from endocrine cells in the lower small intestine, colon and pancreas. PYY inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility (Ref: SWISS-Prot).

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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 light (NF68 or NF-L) is the most abundant of the three proteins.

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NT4 is a member of the neurotrophin family, in knockout animals NT4 deficient mice appeared little changed from wildtype animals, however NT4 is a powerful neurotrophic factor for periferial neuronal ganglia and is capable if sustaining ganglia neurons in vitro. NT4 is closely related to both NGF and BDNF. FUNCTION: Target-derived survival factor for peripheral sensory sympathetic neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Highest levels in prostate, lower levels in thymus, placenta, and skeletal muscle. Expressed in embryonic and adult tissues. SIMILARITY: Belongs to the NGF-beta family.

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Neurofilaments can be defined as the intermediate or 10nm diameter filaments found in neuronal cells. They are composed a mixture of subunits which often includes the neurofilament triplet proteins, NF-L, NF-M and NF-H. Neurofilaments may also include peripherin, alpha-internexin, nestin and in some cases vimentin. Alpha-internexin is a ~66 kDa Class IV intermediate filament subunit expressed in large amounts early in neuronal development, but is downregulated in many neurons as development procedes. Many classes of mature neurons contain alpha-internexin in addition to NF-L, NF-M and NF-H. In some mature neurons alpha-internexin is the only neurofilament subunit expressed. Antibodies to alpha-internexin are therefore unique probes to study and classify neuronal types and follow their processes in sections and in tissue culture. In addition the very early developmental expression of alpha-internexin means its presence is an early and convenient diagnostic feature of neuronal progenitors cells and other cell committed to the neuronal lineage.

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Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. COFACTOR: Binds 2 calcium ions per subunit.

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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.

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Ubiquitin C-terminal hydrolase 1 (UCHL1) has several other names, such as ubiquitin carboxyl esterase L1, ubiquitin thiolesterase, neuron-specific protein PGP9.5 and Park5. It was originally identified as a major component of the neuronal cytoplasm from 2-dimensional gel analysis of brain tissues, and was given the name PGP9.5 (1). The protein is extremely abundant, and was estimated to be present at a concentration of 200-500 µg/g wet weight, representing a major protein component of neuronal cytoplasm (1). This has been claimed to represent 1-2% of total brain protein. It was later found that a ubiquitin C-terminal hydrolase enzyme activity was associated with the PGP9.5 protein, resulting in the renaming of PGP9.5 to ubiquitin C-terminal hydrolase 1.This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. The enzyme also binds to free monoubiquitin and may prevent its degradation in lysosomes.

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FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.

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Endomorphins 1 and 2 are endogenous opioid peptides which have the highest affinity for the mu-opioid receptors. Located in various parts of the brain and interacts with mu-opioid receptors and produces analgesia.

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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 nerurons 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).