Supplier: Biosensis

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

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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.

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

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.

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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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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.

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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.

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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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Peroxiredoxin-1 has a role in redox regulation of the cell.

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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.

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

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

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FUNCTION: Required for autophagy. Conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with nonmuscle actin. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells. INDUCTION: By apoptotic stimuli. PTM: Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane. SIMILARITY: Belongs to the ATG5 family.

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FUNCTION: Nociceptin is the ligand of the opioid receptor-like receptor (OPRL1). It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Expressed predominantly in the spinal cord and brain, being more abundant in the hypothalamus and striatum. Also found in small amounts in ovary. PTM: Specific enzymatic cleavages at paired basic residues probably yield other active peptides besides nociceptin. PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. SIMILARITY: Belongs to the opioid neuropeptide precursor family.

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The 6X His tag is a short peptide sequence of 6 histidine residues. Epitopes such as the 6X His tag are often included with the target DNA at the time of cloning to produce fusion proteins containing the tag sequence. This allows anti-epitope tag antibodies such as this one to serve as a universal detection reagent for any recombinant protein containing this tag. Anti-epitope antibodies are a useful alternative to generating antibodies to identify a specific recombinant protein. The 6X His motif is often used as a tag on recombinant proteins to facilitate purification with immobilized metal-affinity chromatography.

Supplier: Biosensis

The Bcl-2 family of proteins which regulate apoptosis share identical sequences called Bcl-2 Homology domains (BH1-4). The BH3 proteins, including BID, NOXA, PUMA, BIK, BIM and BAD are all pro-apoptotic and share sequence identity within the amphipathic alpha-helical BH3 region, which is essential for their apoptotic function. NOXA is highly expressed in adult T-cell leukemia cell line.

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Arc (also termed activity-regulated cytoskeleton-associated protein or Arg3.1), is an effector immediate early gene whose upregulation has been demonstrated during events of synaptic plasticity. Arg3.1 expression is detectable in neuronal cell bodies and dendrites in the brain regions including striatum and cortex hippocampus, hypothalamus, amygdala.

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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.

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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.

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Maltose binding protein (MBP) is encoded by the malE gene of E.coli. MBP is often used in protein expression studies because it creates a stable fusion product that does not appear to interfere with the bioactivity of the protein of interest. It also allows for its easy purification from bacterial extracts under mild conditions.

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The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

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Protein DJ-1 has many roles including protecting cells against oxidative stress and cell death (Ref: SwissProt). Mutations in the DJ-1 gene have been associated with rare forms of autosomal recessive early-onset Parkinson's disease.

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Peripherin is a class-III neuronal intermediate filament protein found in certain classes of neuron, most of which are located in the peripheral nervous system.

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Nerve growth factor (NGF) is synthesized as a precursor (proNGF) which may be released and have physiological functions to cause cell death. It binds neurotrophin receptor p75 and sortilin and may also be important for the development of nervous system. proNGF is synthesized in target tissues and glia, transported retrogradely and may be released. This antibody is raised in sheep to detect the prodomain of NGF not the mature peptide.

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TISSUE SPECIFICITY: Predominantly expressed in trigeminal and dorsal root sensory ganglia. Isoform 1 and isoform 3 are also expressed in brain and peripheral blood mononuclear cells.

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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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Beclin-1 plays a central role in autophagy. It may also play a role in antiviral host defense. It is ubiquitously expressed and it localises to the cytoplasm, golgi apparatus membrane, and in dendrites and cell bodies of cerbellar Purkinje cells. The unprocessed precursor has a length of 450 amino acids and an estimated molecular weight of 51.89 kDa.

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14.3.3 protein eta or 14.3.3  binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (Ref SwissProt). 14.3.3 protein eta is widely expressed as both homodimers and heterodimers and are concentrated in the nervous system. High concentrations of 14.3.3 protein eta have been linked to Creutzfeld Jacob Disease, Parkinson's Disease and early-onset schizopherenia.

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Vimentins are class-III intermediate filaments specific to mesenchymal tissue. Vimentin is an important cytoskeletal component responsible for maintaining cell integrity and has a probable role in the intracellular transport of proteins such as lipoproteins between the nucleus and plasma membrane. Immunohistochemical staining for Vimentin is characteristic of sarcomas.