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Artikel-Nr: (BOSSBS-11341R-HRP)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-HRP
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-A488)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-A488
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-A680)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-A680
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-A647)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-A647
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11395R-A555)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11395R-A555
Beschreibung: Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAPs (soluble NSF attachment proteins) and Synaptotagmin. Endobrevin, also designated VAMP-8 or ED, is a 100 amino acid single-pass type IV membrane protein that belongs to the synaptobrevin family. Similar in sequence to the synaptobrevins, endobrevin is abundantly expressed in kidney, moderately expressed in heart and spleen, and slightly expressed in brain, thymus and liver. Endobrevin interacts specifically with the SNAPs, most likely through an endobrevin-containing SNARE complex.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11395R-FITC)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11395R-FITC
Beschreibung: Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAPs (soluble NSF attachment proteins) and Synaptotagmin. Endobrevin, also designated VAMP-8 or ED, is a 100 amino acid single-pass type IV membrane protein that belongs to the synaptobrevin family. Similar in sequence to the synaptobrevins, endobrevin is abundantly expressed in kidney, moderately expressed in heart and spleen, and slightly expressed in brain, thymus and liver. Endobrevin interacts specifically with the SNAPs, most likely through an endobrevin-containing SNARE complex.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11395R-A647)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11395R-A647
Beschreibung: Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAPs (soluble NSF attachment proteins) and Synaptotagmin. Endobrevin, also designated VAMP-8 or ED, is a 100 amino acid single-pass type IV membrane protein that belongs to the synaptobrevin family. Similar in sequence to the synaptobrevins, endobrevin is abundantly expressed in kidney, moderately expressed in heart and spleen, and slightly expressed in brain, thymus and liver. Endobrevin interacts specifically with the SNAPs, most likely through an endobrevin-containing SNARE complex.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-CY5)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-CY5
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-A350)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-A350
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R-A750)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R-A750
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-11341R)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-11341R
Beschreibung: Complexin 1 and Complexin 2, also designated Synaphin 1 and Synaphin 2, contain an a-helical middle domain of approximately 58 amino acids. Complexin 1 and Complexin 2 are expressed in presynaptic terminals of inhibitory and excitatory hippocampal neurons, respectively, and in cytoplasmic pools during early stages of development. Complexins promote SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplex formation by binding to synaxin with its a-helical domain. Complexins are important regulators of transmitter release at a late step in calcium dependent neurotransmitter release or immediately after the calcium-triggering step of fast synchronous transmitter release and preceding vesicle fusion. Neurons lacking complexins show reduced transmitter release efficiency due to decreased calcium sensitivity of the synaptic secretion process. Complexin 2 may play a role in LTP (long term potentiation) following tetanic stimulation. A progressive loss of Complexin 2 occurs in the brains of mice carrying the Huntington disease mutation, an autosomal dominant neurodegenerative disorder. Changes in the neurotransmitter release might contribute to the motor, emotional and cognitive dysfunctions seen in these mice.
UOM: 1 * 100 µl


Artikel-Nr: (PRSI92-103)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 92-103
Beschreibung: Cysteine Protease ATG4A (ATG4A) is a cytoplasmic protein that belongs to the peptidase C54 family. ATG4A is widely expressed in many tissues at a low level, but the highest expression is observed in skeletal muscle and brain. ATG4A is a cysteine protease required for autophagy; it cleaves the C-terminal part of MAP1LC3, GABARAPL2 or GABARAP. ATG4A is inhibited by N-ethylmaleimide. It is suggested that ATG4A has a significant role in suppressing various cancers.
UOM: 1 * 50 µG


Artikel-Nr: (PRSI92-579)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 92-579
Beschreibung: Syntaxin 7 (STX7) is a member of a family of membrane-trafficking proteins named as soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), and mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes. Syntaxin-7 has been shown to be present in both late endosomes and lysosomes, and to be required for both homotypic late endosome fusion and heterotypic fusion with lysosomes. STX7 has been shown to interact with STX8, VPS18, Vesicle-associated membrane protein 8 and VPS11.
UOM: 1 * 50 µG


Artikel-Nr: (PRSI6929)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 6929
Beschreibung: VAMP7 Antibody: VAMP7 is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family, localizing to late endosomes and lysosomes. VAMP7 is thought to mediate the fusion of endosomes to their target lysosomes as well as other exocytosis events during phagocytosis and neuritogenesis. VAMP7 interacts with the VPS9 ankyrin repeat protein VARP, a protein that localizes to early endosomes and thought to regulate endosome dynamics. Together with CD82, VAMP7 can modulate the signaling of EGFR by regulating its endocytosis from the plasma membrane.
UOM: 1 * 100 µG


Artikel-Nr: (BSBTPB10017)
Lieferant: Boster Bio
Hersteller Artikel Nummer : PB10017
Beschreibung: Vesicle-associated membrane protein 7 (VAMP-7), also known as SYBL1, is a protein that in humans is encoded by the VAMP7 gene. This gene encodes a transmembrane protein that is a member of the soluble N-ethylmaleimide- sensitive factor attachment protein receptor (SNARE) family. The encoded protein localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. Alternate splicing results in multiple transcript variants.
UOM: 1 * 100 µG


Artikel-Nr: (PRSI92-044)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 92-044
Beschreibung: Cysteine Protease ATG4C (ATG4C) belongs to the peptidase C54 family. It is required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form which is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. ATG4C is a cytoplasmic protein and high expressed in skeletal muscle, liver, testis and heart. ATG4C can be inhibited by N-ethylmaleimide.
UOM: 1 * 50 µG


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