You Searched For: Biosensis

Catalog Number: (10782-046)

Supplier: Biosensis

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

Catalog Number: (10782-598)

Supplier: Biosensis

Description: 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).

Catalog Number: (10782-626)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-622)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-100)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-096)

Supplier: Biosensis

Description: Spectrins are a family of filamentous cytoskeletal proteins that function as essential scaffold proteins that stabilize the plasma membrane and organize intracellular organelles. The Spectrins form into dimers and further into tetramers of alpha and beta subunits (Ref: Entrez Gene). The alpha-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons.

Catalog Number: (10782-400)

Supplier: Biosensis

Description: FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. SUBCELLULAR LOCATION: Endoplasmic reticulum; rough endoplasmic reticulum. Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. SIMILARITY: Belongs to the orexin family.

Catalog Number: (10782-424)

Supplier: Biosensis

Description: Synuclein alpha interacting protein (Synphilin-1) contains several protein-protein interaction domains and interacts with alpha synuclein in neurons. Mutations of SNCAIP have been linked to Parkinson disease. The amino acid sequence of synphilin-1 shares a high level of identity with its human counterpart, particularly in regions containing ankyrin-like motifs and the coiled-coil domain. Expression pattern of synphilin-1 in tissues is similar in both mouse and human. Synphilin-1 has an important role in the formation of aggregates and cytotoxicity in Parkinson disease and also Dorfin may be involved in the pathogenic process by ubiquitylation of synphilin-1.

Catalog Number: (10782-404)

Supplier: Biosensis

Description: The neural adhesion molecule Contactin-6, also known as NB-3, is a contactin/F3 subgroup member of immunoglobulin superfamily. It is expressed exclusively in the nervous system and mainly upregulated at the early postnatal stage during mouse brain development. Employing Northern blot analysis Kamei et al found that amongst different regions of the adult human nervous system cerebellum expressed highest level of NB-3 mRNA. The expression of NB-3 in the cerebellum increases until adulthood. In contrast, the expression in the cerebrum declines to a low level after postnatal day 7. NB-3 like other neural recognition molecules plays a vitally important role in axonal guidance during development, plasticity, and maintenance of synaptic connections in the adult brain. Cui et al recently showed that NB-3 acts as a novel Notch ligand to participate in oligodendrocyte generation. Furthermore, NB-3 triggers nuclear translocation of the Notch intracellular domain and promotes oligodendrogliogenesis from progenitor cells and differentiation of oligodendrocyte precursor cells via Deltex1. In primary oligodendrocytes, NB-3 increases myelin-associated glycoprotein transcripts. Hence, the NB-3/Notch signaling pathway may be worthwhile a closer examination for its potential for the treatment of demyelinating diseases. Human NB-3 shares with rat NB-3 86% identity in nucleotide sequences and 90% identity in amino acid sequences. FUNCTION: Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Involved in motor coordination. SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Expressed in brain. In brain, it is preferentially expressed in the accessory olfactory bulb, layers II/III and V of the cerebral cortex, piriform cortex, anterior thalamic nuclei, locus coeruleus of the pons and mesencephalic trigeminal nucleus and in Purkinje cells of the cerebellum.

Catalog Number: (10782-060)

Supplier: Biosensis

Description: GFAP is a 50 kDa intra-cytoplasmic filamentous protein of the cytoskeleton in astrocytes. During the development of the central nervous system, it is a cell-specific marker that distinguishes astrocytes from other glial cells. GFAP immunoreactivity has been shown in immature oligodendrocytes, epiglottic cartilage, pituicytes, papillary meningiomas, myoepithelial cells of the breast and in non-CNS: Schwann cells, salivary gland neoplasms, enteric glia cells, and metastasizing renal carcinomas.

Catalog Number: (10782-416)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-392)

Supplier: Biosensis

Description: CNTF is a survival promoting factor for different types of neurons in vitro and in vivo. The essential structural features for the biological function of human CNTF were investigated by Thier, M. et al. They showed that deletion of 14 N-terminal and 18 C-terminal amino acids significantly increased bioactivity compared to wild-type CNTF. FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Nervous system. PHARMACEUTICAL: CNTF is being tested under the name Axokine by Regeneron Pharmaceuticals for treatment of human motor neuron diseases, such as amyotrophic lateral sclerosis (ALS). As it induces substantial weight loss, preferentially of fat as opposed to lean body mass, it is being used for obesity treatment. SIMILARITY: Belongs to the CNTF family.

Catalog Number: (10782-432)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-074)

Supplier: Biosensis

Description: 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.

Catalog Number: (10782-068)

Supplier: Biosensis

Description: Nestin is a member of the class IV intermediate filament protein family which is expressed in neuronal stem cells. The molecular weight of human Nestin as determined by SDS-PAGE mobility is about 240kDa. However the real molecular weight is considerably less than this, at 177kDa, the disparity being likely due to the highly charged region of the C-terminal segment. Nestin is relatively poorly conserved in protein sequence across species boundaries, so that the mouse and human proteins have an overall identity of only 62%. As a result antibodies to the human protein often fail to recognize the rodent homologue and vice versa. However this antibody stains both rodent and human Nestin. Antibodies to Nestin are widely used to identify neural stem cells.

Catalog Number: (10782-070)

Supplier: Biosensis

Description: 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.