622 Results for: "Biosensis"

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Leptin is secreted by white adipocytes and functions as part of a signaling pathway that can inhibit food intake and/or regulate energy expenditure to maintain constancy of the adipose mass. Leptin has a variety of other roles including endocrine functions, regulation of immune and inflammatory responses, hematopoiesis, angiogenesis and wound healing (Ref Entrez Gene).

Supplier: Biosensis

Human Methionine enkephalin (Met-Enkephalin) is a small 5 amino acid peptide cleaved from the precursor pro-opiomelanocortin (POMC). Met-Enkephalin is an endogenous opioid peptide that interacts with opioid receptors and produces analgesic effects.

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Peroxiredoxin-2 has a role in redox regulation of the cell.

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.

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

Supplier: Biosensis

Leptin is secreted by white adipocytes and functions as part of a signaling pathway that can inhibit food intake and/or regulate energy expenditure to maintain constancy of the adipose mass. Leptin also has several endocrine functions and is involved in the regulation of immune and inflammatory responses, hematopoiesis, angiogenesis and wound healing (Ref: Entrez Gene).

Supplier: Biosensis

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. Peripherin is a ~57kDa intermediate filament subunit found initially in sensory neurons of the peripheral nervous systems, which gives the protein its name. The HGNC name for this protein is PRPH. Subsequently, peripherin was found in some sensory and other neurons of the central nervous system and also in rat pheochromacytoma PC12 cells. Peripherin is also expressed in certain neuroendocrine tumors and in the insulin producing cells of the pancreas. Peripherin belongs to the Class III family of intermediate filament subunits which also includes vimentin, glial fibrillary acidic protein (GFAP) and desmin.

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Glial fibrillary acidic protein (GFAP) is approx. 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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Hormone Sensitive Lipase (HSL) hydrolyzes stored triglycerides to free fatty acids in adipose tissue and heart. In steroidogenic tissues, HSL principally converts cholesteryl esters to free cholesterol for steroid hormone production (ref: SWISSPROT).

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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.

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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.

Supplier: Biosensis

Leptin is secreted by white adipocytes and functions as part of a signaling pathway that can inhibit food intake and/or regulate energy expenditure to maintain constancy of the adipose mass. Leptin also has several endocrine functions and is involved in the regulation of immune and inflammatory responses, hematopoiesis, angiogenesis and wound healing (Ref: Entrez Gene) .

Supplier: Biosensis

CATALYTIC ACTIVITY: ATP + H2O = ADP + phosphate. SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By similarity). ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. SIMILARITY: Belongs to the cation transport ATPase (P-type) family. Type V subfamily.

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Responses evoked by low pH and heat, and capsaicin can be antagonized by capsazepine. SIMILARITY: Belongs to the transient receptor family. TrpV subfamily. SIMILARITY: Contains 3 ANK repeats.

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FUNCTION: Seems to promotes the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family.

Supplier: Biosensis

Peroxisome proliferator-activated receptor gamma (PPARG) is a nuclear hormone receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription (Ref: SWISSPROT).

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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.

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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.

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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).