You Searched For: N-Ethylmaleimide

Catalog Number: (BOSSBS-11395R-CY3)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-11395R-A680)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-11395R-A750)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-12465R-A350)

Supplier: Bioss

Description: 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 have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also designated synaptobrevins), including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12465R-CY5)

Supplier: Bioss

Description: 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 have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also designated synaptobrevins), including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11875R-A647)

Supplier: Bioss

Description: Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg2+ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyzes lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11875R-A555)

Supplier: Bioss

Description: Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg2+ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyzes lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11875R-A680)

Supplier: Bioss

Description: Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg²⁺ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyses lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11875R-CY3)

Supplier: Bioss

Description: Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg2+ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyzes lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11341R-CY3)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-11341R-CY7)

Supplier: Bioss

Description: 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

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Catalog Number: (BOSSBS-11255R-A488)

Supplier: Bioss

Description: Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11255R-HRP)

Supplier: Bioss

Description: Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12465R-A680)

Supplier: Bioss

Description: 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 have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25 kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also designated synaptobrevins), including VAMP-1 and VAMP-2, and synaptotagmin, a protein that may function as an inhibitor of exocytosis, are vesicular proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11364R-A647)

Supplier: Bioss

Description: The protein encoded by this gene is a coiled-coil-forming protein that associates with the SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complex of proteins and the BLOC-1 (biogenesis of lysosome-related organelles) complex. Biochemical studies have identified additional binding partners. As part of the SNARE complex, it is required for vesicle docking and fusion and regulates neurotransmitter release. The BLOC-1 complex is required for the biogenesis of specialized organelles such as melanosomes and platelet dense granules. Mutations in gene products that form the BLOC-1 complex have been identified in mouse strains that are models of Hermansky-Pudlak syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2012].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11341R-A488)

Supplier: Bioss

Description: 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

Sale