622 Results for: "Biosensis"

Supplier: Biosensis

BDNF belongs to the neurotrophin family and regulates the survival and differentiation of neurons during development. 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.FUNCTION: Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. 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. 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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Neurturin (NTN) is a member of the GDNF family of neurotrophic factors. This protein is a potent survival factor for several populations of central and peripheral neurons in mature and developing rodents. FUNCTION: Supports the survival of sympathetic neurons in culture. May regulate the development and maintenance of the CNS. Might control the size of non-neuronal cell population such as haemopoietic cells. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. DISEASE: Defects in NRTN are a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, and possibly with other loci, defects in NRTN are 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. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.

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FUNCTION: Ubiquitin-like protein which binds to a wide range of target proteins. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved in targeting RANGAP1 to the nuclear pore complex protein RANBP2. SUBUNIT: Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. SUBCELLULAR LOCATION: Nucleus; nuclear membrane. Nucleus; nucleoplasm; nuclear speckle. Cytoplasm. SIMILARITY: Belongs to the ubiquitin family. SMT3 subfamily. SIMILARITY: Contains 1 ubiquitin-like domain.

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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.

Supplier: Biosensis

FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. COFACTOR: Binds 1 zinc ion per subunit. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. DISEASE: Defects in SOD1 are the cause of familial amyotrophic lateral sclerosis (FALS); also called amyotrophic lateral sclerosis 1 (ALS1 or ALS). ALS is a degenerative disorder of motorneurons in the cortex, brainstem and spinal cord. ALS is characterized by muscular weakness and atrophy beginning in the hands and spreading to the forearms and legs. Muscle fasciculations are commonly visible. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. ALS is sometimes referred to as Lou Gehrig disease after the famous American baseball player who was diagnosed with the disorder. FALS, the familial form of ALS, accounts for about 10% of the cases and is transmitted in an autosomal dominant manner. The mean age at onset of FALS is 45 years. MISCELLANEOUS: Zinc binding promotes dimerization. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.

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FUNCTION: Probably involved in formation of autophagosomal vacuoles (autophagosomes). SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. SUBCELLULAR LOCATION: LC3-I: Cytoplasm. LC3-II: Intracytoplasmic membrane; lipid-anchor. LC3-II binds to the autophagic membranes. TISSUE SPECIFICITY: Most abundant in placenta, lung and ovary. PTM: The precursor molecule is cleaved by APG4B/ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II. SIMILARITY: Belongs to the MAP1 LC3 family.

Supplier: Biosensis

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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Human beta-Lipotropin is a 93 amino acid polypeptide that is cleaved from carboxy-terminal fragment of the precursor pro-opiomelanocortin (POMC). It stimulates melanocytes to produce melanin, and can also be cleaved into smaller peptides including opioid peptides: gamma-lipotropin, alpha-MSH, beta-MSH, gamma-MSH, alpha-endorphin, beta-endorphin, gamma-endorphin and met-enkephalin

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Adrenocorticotropic hormone (ACTH) is cleaved from the precursor pro-opiomelanocortin (POMC). The hormone is produced and secreted by the pituitary gland and stimulates release of cortisol by adrenal glands.

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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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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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Superoxide dismutase [Mn], mitochondrial destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (Ref: SwissProt).

Supplier: Biosensis

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.

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SUMO-1 binds to a wide range of target proteins as part of a post-translational modification system. Unlike ubiquitin, it does not seem to target protein for degradation, but is involved in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis, apoptosis, protein stability and signal transduction. SUBUNIT: Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. SUBCELLULAR LOCATION: Nucleus; nuclear membrane. Nucleus; nucleoplasm; nuclear speckle. Cytoplasm. SIMILARITY: Belongs to the ubiquitin family. SMT3 subfamily. SIMILARITY: Contains 1 ubiquitin-like domain. PTM: Cleavage of the last four amino acids of the carboxy-terminus of the precursor form by SENP1 or SENP2 is necessary for function. Several pseudogenes have been reported as well as a number of alternatively spliced isoforms.

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FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. SUBUNIT: Heterodimer. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with MAFB. SUBCELLULAR LOCATION: Nucleus. INDUCTION: C-fos expression increases upon a variety of stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, stress and cell injury. SIMILARITY: Belongs to the bZIP family. Fos subfamily. SIMILARITY: Contains 1 bZIP domain

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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.

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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.

Supplier: Biosensis

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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Coronins belong to the WD40 or WD family of proteins. Coronins appear to be particularly involved in binding to actin, actin associated proteins, tubulin and phospholipase C and have been implicated in the mechanisms of chemotaxis and phagocytosis. In mammals there are at least five major coronin proteins, named coronins 1 to 5 in one nomenclature. Another nomenclature divides these five proteins in coronins 1a and 1b, 2a, 2b and 2c (see the Human Genone Organization Gene Nomenclature Committee link for this family). The mammalian coronin family members are abundant components of eukaryotic cells and each type has a restricted cell type specific expression pattern. Coronin 1A is found exclusively in hematopoetic lineage cells such as lymphocytes, macrophages and neutrophils. This antibody is therefore an excellent marker of cells of this lineage and can also be used to study the leading edges particularly of neutrophils. Since the only hematopoetic cells found within the central nervous system are microglia, this antibody is also an excellent marker of this important cell type. Microglia are numerically fairly minor components of the nervous system, but microglial activation is seen in response to a wide variety of damage and disease states, including ALS, Alzheimer's disease and responses to brain tumors. Since coronin 1a is a constitutive component of microglia, the coronin 1a antibody can be used to study both quiescent and activated microglia.

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DBH is an oxireductase belonging to the copper type II ascorbate-dependent monooxygenase family. DBH exists as a homotetramer composed of two non-covalently bound disulfide-linked dimers. It is present in the synaptic vesicles of postganglionic sympathetic neurons and converts dopamine to norepinephrine. It binds 2 copper ions and 1 PQQ per subunit . Depending on the presence of a signal peptide, DBH can exist in both soluble and membrane-bound forms.

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.

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Human beta-endorphin is a 31 amino acid peptide cleaved from the precursor pro-opiomelanocortin (POMC). It is an endogenous opioid peptide neurotransmitter that interacts with opioid receptors.

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LRRK2 is a member of the leucine-rich repeat kinase family. Its role is yet unknown but it may play a role in the phoshorylation of proteins central to parkinson diseases. LRRK2 contains an ankryin repeat region, a leucine-rich repeat (LRR) domain, a kinase domain, a DFG-like motif, a RAS domain, a GTPase domain, a MLK-like domain and a WD40 domain. LRRK2 is present in the cytoplasm but also associates with the mitochondrial outer membrane. Defects in LRRK2 are the cause of Parkinson disease 8 (PARK8). Parkinson disease is characterised by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK8 is an autosomal-dominant late-onset parkinsonism, characterized by onset from 50 to 65 years, with slow progression and relatively benign course.

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ATG10 plays a role in autophagy. It is an E2-like enzyme involved in 2 ubiquitin-like modifications essential for autophagosome formation: ATG12-ATG5 conjugations and modificatioon of a soluble form of MAPLC3 1A, a homolog of yeast ATG8, to a membrane bound form.  It is also able to directly interact either with ATG5 or ATG7.

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

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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).

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Nerve growth factor receptor (NGFR) is also referred to as p75(NTR) due to its molecular mass and its ability to bind at low affinity not only NGF (see 162030), but also other neurotrophins, including brain-derived neurotrophic factor (BDNF; 113505), neurotrophin-3 (NTF3; 162660), and neurotrophin-4/5 (NTF5; 162662). At the time of its discovery, NGFR was considered a unique type of protein. Subsequently, however, a large superfamily of tumor necrosis factor receptors were found to share the overall structure of NGFR (4 extracellular ligand-binding, cysteine-rich repeats, or CRs, and signaling through association with, or disassociation from, cytoplasmic interactors). The identification of this superfamily helped elucidate some of the biologic functions of NGFR, including its ultimate involvement in the nuclear factor kappa-B (NFKB; see 164011) and apoptosis pathways. As a monomer, NGFR binds NGF with low affinity. Higher affinity binding is achieved by association with higher molecular mass, low-affinity neurotrophin receptors, namely the tropomyosin receptor kinases, TRKA (NTRK1; 191315), TRKB (NTRK2; 600456), and TRKC (NTRK3; 191316). TRKA, TRKB, and TRKC are specific for or 'preferred by' NGF, NTF5 and BDNF, and NTF3, respectively. NTF3 also binds to TRKA and TRKB, but with significantly lower affinity.

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The V5 epitope corresponds to a region from Simian Virus Type 5 (SV5).

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Fox3 is one of a family of mammalian homologues of Fox-1. The Fox proteins are about 46kDa in size, and each includes a central highly conserved RRM type RNA recognition motif. Much interest has focused on Fox3 as a result of the recent finding that this protein corresponds to NeuN, a neuronal nuclear antigen. NeuN/Fox-3 has a function in RNA splicing and is expressed heavily and specifically in neuronal nuclei and cytoplasm. Our antibody was raised against the N-terminal 100 amino acids of human Fox3 as expressed in and purified from E. coli. We did not use full length Fox3 as immunogen since the three mammalian Fox homologues, namely Fox1, Fox2 and Fox3, include virtually identical RRM motifs. The N-terminal region of the three molecules are much more variable in the three molecules so antibodies specific for each of the three molecules can therefore be generated.

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