You Searched For: N-Ethylmaleimide

Supplier: Thermo Scientific

Description: N-Ethylmaleimide (NEM) 99+%

MSDS

Supplier: Thermo Scientific

Description: N-Ethylmaleimide (NEM) 99+%

MSDS Certificates

Supplier: Thermo Scientific

Description: N-Ethylmaleimide (NEM) ≥98%

MSDS Certificates

Catalog Number: (ENZOADIVAMSV020D)

Supplier: ENZO LIFE SCIENCES

Description: N-ethylmaleimide-sensitive factor (NSF) is involved in a variety of membrane fusion events and plays a prominent role in synaptic vesicle fusion. In order to interact with target membranes, NSF requires another set of soluble proteins called Soluble NSF attachment proteins (SNAPs). Together with synaptotagmin and alpha-SNAP, NSF modulates the interaction of SNAP25, VAMP, and syntaxin in an ATP-dependent manner to form a 20S complex involved in synaptic vesicle docking and fusion.

UOM: 1 * 50 µG

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Catalog Number: (USBIE8608-71)

Supplier: US Biological

Description: Anti-N-Ethylmaleimide Sensitive Factor Attachment Protein, gamma Chicken Polyclonal Antibody

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-12465R)

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-A555)

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-HRP)

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-11364R-A680)

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 specialised 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13493R-FITC)

Supplier: Bioss

Description: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11364R-CY3)

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-11364R-A350)

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-11395R-A488)

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-CY7)

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-A647)

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-11255R-CY5)

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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