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Katalogové číslo: (BOSSBS-11395R-A750)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11395R-A680)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-FITC)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11395R-FITC)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11395R-A555)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11395R-A647)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-CY3)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-CY7)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-A488)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-A555)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-HRP)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-A680)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-A647)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (USBI130141)
Dodavatel: US Biological
Popis: Anti-NAPG Mouse Monoclonal Antibody [clone: 4B5]
Měrná jednotka: 1 * 100 µG


Katalogové číslo: (BOSSBS-11341R-CY5)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11341R-A750)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


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Omezené množství produktu na skladě. Zboží může být k dispozici v jiném skladě poblíž vašeho sídla. Přesvědčte se, že jste přihlášení na stránky, abyste mohli vidět dostupné položky na skladě. Pokud je stále zobrazeno call a potřebujete asistenci, volejte na číslo 321 570 321.
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