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Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
Numéro de catalogue:
(BOSSBS-11988R-CY5)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-A680)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development. Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation. Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells. Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain. Neurabin II localizes to neuronal dentritic spines, which are the specialised protrusions from dendritic shafts that receive most of the excitatory input in the CNS. Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells. Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis. Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11498R-HRP)
Fournisseur:
Bioss
Description:
Olfactory sensory neurons contain olfactory receptors, which are G protein-coupled receptor proteins that localize to the cilia and display affinity for and bind to a variety of odor molecules. Olfactory neurons send their axons from the olfactory epithelium to the olfactory bulb, which is covered by the CNS basal lamina. FEZF1 (Fez family zinc finger protein 1), also known as Forebrain Embryonic Zinc Finger and Zinc finger protein 312B, is a 475 amino acid nuclear protein that is expressed in the olfactory epithelium and hypothalamus of mice. In FEZF1-deficient mice, axons of olfactory neurons do not reach the olfactory bulb, suggesting that FEXF1 is required for the penetration of olfactory axons though the basal lamina before innervation of the olfactory bulb. When FEZF1 translocates to the nucleus, it induces KRAS overexpression, resulting in activation of ERK-signaling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumor mass in mice. There are three isoforms of FEZF1 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11498R-A647)
Fournisseur:
Bioss
Description:
Olfactory sensory neurons contain olfactory receptors, which are G protein-coupled receptor proteins that localize to the cilia and display affinity for and bind to a variety of odor molecules. Olfactory neurons send their axons from the olfactory epithelium to the olfactory bulb, which is covered by the CNS basal lamina. FEZF1 (Fez family zinc finger protein 1), also known as Forebrain Embryonic Zinc Finger and Zinc finger protein 312B, is a 475 amino acid nuclear protein that is expressed in the olfactory epithelium and hypothalamus of mice. In FEZF1-deficient mice, axons of olfactory neurons do not reach the olfactory bulb, suggesting that FEXF1 is required for the penetration of olfactory axons though the basal lamina before innervation of the olfactory bulb. When FEZF1 translocates to the nucleus, it induces KRAS overexpression, resulting in activation of ERK-signaling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumor mass in mice. There are three isoforms of FEZF1 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11498R-A488)
Fournisseur:
Bioss
Description:
Olfactory sensory neurons contain olfactory receptors, which are G protein-coupled receptor proteins that localize to the cilia and display affinity for and bind to a variety of odor molecules. Olfactory neurons send their axons from the olfactory epithelium to the olfactory bulb, which is covered by the CNS basal lamina. FEZF1 (Fez family zinc finger protein 1), also known as Forebrain Embryonic Zinc Finger and Zinc finger protein 312B, is a 475 amino acid nuclear protein that is expressed in the olfactory epithelium and hypothalamus of mice. In FEZF1-deficient mice, axons of olfactory neurons do not reach the olfactory bulb, suggesting that FEXF1 is required for the penetration of olfactory axons though the basal lamina before innervation of the olfactory bulb. When FEZF1 translocates to the nucleus, it induces KRAS overexpression, resulting in activation of ERK-signaling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumor mass in mice. There are three isoforms of FEZF1 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13597R-A647)
Fournisseur:
Bioss
Description:
The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-A680)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localised to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-CY7)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-HRP)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11498R-A350)
Fournisseur:
Bioss
Description:
Olfactory sensory neurons contain olfactory receptors, which are G protein-coupled receptor proteins that localize to the cilia and display affinity for and bind to a variety of odor molecules. Olfactory neurons send their axons from the olfactory epithelium to the olfactory bulb, which is covered by the CNS basal lamina. FEZF1 (Fez family zinc finger protein 1), also known as Forebrain Embryonic Zinc Finger and Zinc finger protein 312B, is a 475 amino acid nuclear protein that is expressed in the olfactory epithelium and hypothalamus of mice. In FEZF1-deficient mice, axons of olfactory neurons do not reach the olfactory bulb, suggesting that FEXF1 is required for the penetration of olfactory axons though the basal lamina before innervation of the olfactory bulb. When FEZF1 translocates to the nucleus, it induces KRAS overexpression, resulting in activation of ERK-signaling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumor mass in mice. There are three isoforms of FEZF1 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(735-0274)
Fournisseur:
Thermo Fisher Scientific
Description:
Les processeurs de particules magnétiques KingFisher™ sont conçus pour automatiser le traitement fastidieux des échantillons d'acides nucléiques, de protéines ou de cellules de pratiquement n'importe quelle source (sang, cultures cellulaires, lysats tissulaires, sol, selles, par exemple). La gamme KingFisher™ se compose de quatre instruments présentant des rendements et des capacités de volume différents pour répondre aux divers besoins de traitement d'échantillons. Chaque système est constitué d'un instrument, de consommables spécifiques et d'un logiciel. Les systèmes KingFisher™ offrent une purification de haute qualité, rapide et reproductible de l'ADN, de l'ARN, des protéines et des cellules pour divers types d'applications en aval, y compris la génomique et la protéomique, le dépistage des drogues, la médecine légale, la détection des biomarqueurs, le contrôle qualité et les tests vétérinaires.
UOM:
1 * 1 ST
Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
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