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Rat Snare Complex

Also showing Rat Snap Receptor Activity

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Vesicle transport through interaction with t-SNAREs homolog 1 (Vti1) has two protein members, Vti1a and Vti1b. Human Vti1 was first identified as a homolog of the yeast v-SNARE Vti1p and was able to functionally rescue the phenotype of Vti1p-deficient yeast (1). The mammalian proteins Vti1a and Vti1b exhibit distinct but overlapping localization. Vti1a and Vti1b are both localized in the trans-Golgi network, with Vti1a also found in the Golgi apparatus and Vti1b in endosomes (2). Vti1 proteins have been implicated in a number of protein-protein interactions with partners such as VAMP4, syntaxin 6, syntaxin 8, syntaxin 16, and synaptobrevin (2-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Vesicle-associated membrane protein 2 (VAMP2, also called synaptobrevin) is part of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex (1). The SNARE complex is involved in vesicular transport and membrane fusion, a process regulated by calcium (2). In neurons, VAMP2 is predominantly inserted in presynaptic vesicle membranes. Assembly of VAMP2 with the plasma membrane SNAREs syntaxin 1 and SNAP25 is a key event necessary for membrane fusion and neurotransmitter release (2). In addition to this important function, VAMP2 is also involved in granule exocytosis in neutrophils (3) and release of bioactive peptides from cardiac myocytes (4) and juxtaglomerular cells (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Vesicle-associated membrane protein 1 (VAMP1), also called synaptobrevin 1, is part of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex (1). The SNARE complex is involved in calcium regulated vesicular transport and membrane fusion (2). While related protein VAMP2 exhibits a wider distribution and is more abundant in the brain, VAMP1 is the main isoform in specific brain regions including the subthalamus nucleus zona incerta (1), the ostral periolivary region, and the retina (3). In addition, VAMP1 is involved in neurotransmitter release at the neuromuscular junction (4) and in the release of bioactive peptides from cardiac myocytes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 3 (VAMP3), also known as cellubrevin, has a broad tissue distribution and localizes to endosomal compartments (3). VAMP3 interacts with the t-SNAREs syntaxin1, syntaxin4, SNAP23, and SNAP25 (4,5). Research studies indicate that VAMP3 is involved in transferrin receptor recycling to the plasma membrane (6) and in T-cell receptor recycling to immunological synapses (7). Inhibition of VAMP3 with tetanus toxin impairs membrane trafficking during cell migration (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Syntaxin 1A (STX1A) is a SNARE protein involved in intracellular membrane fusion, including synaptic vesicle fusion (1). At the synapse, syntaxin 1 is located at the presynaptic plasma membrane and is therefore categorized as a t-SNARE protein (2). The amino-terminal domain of syntaxin 1 interacts with Munc18-1 and this interaction is essential for synaptic vesicle fusion (3). Although originally characterized from neural tissues, research studies have demonstrated syntaxin 1A expression in exocrine tissues such as pancreatic islets (4) where it negatively regulates insulin release (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The membrane protein syntaxin 5 (STX5) is a key component of soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) complexes that regulate cellular protein transport, vesicle docking, and membrane fusion (1). Syntaxin 5 protein is found as a 42 kDa ("long") protein localized to the Golgi complex and endoplasmic reticulum, and a “short” 35 kDa isoform localized primarily to the Golgi (2,3). Formation of the syntaxin 5 SNARE complex, which also includes proteins Sec22B, Bet1, GOSR1, GOSR2, and Ykt6, allows for regulation of ER-to-Golgi transport, intra-Golgi transport, and endosome-to-Golgi retrograde transport (4-6). Research studies indicate that the syntaxin 5 SNARE complex also plays an essential role in autophagy following autophagosome formation. Intracellular protein transport mediated by the syntaxin 5 complex is required for transport and localized activity of lysosomal proteases. The experimental reduction or deletion of syntaxin 5 complex components results in non-functional lysosomes and accumulation of autophagosomes (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion that pair vesicular SNAREs (v-SNAREs) with cognate target SNARE (t-SNARE) proteins (reviewed in 1,2). Vesicle-associated membrane protein 7 (VAMP7), or tetanus neurotoxin-insensitive VAMP (TI-VAMP), is a widely expressed v-SNARE involved in exocytosis of granules and synaptic vesicles in various cell types, membrane remodeling, neurite outgrowth, lysosomal secretion, and autophagosome maturation (3). Activity of VAMP7 can be regulated by c-Src-mediated tyrosine phosphorylation, which activates VAMP7-mediated exocytosis (4). VAMP7 activity can also be regulated through interaction with the guanine nucleotide exchange factor Varp (5,6). Several research studies indicate that VAMP7 plays an important role in neurite outgrowth as well as potential neurological activities, including anxiety (7-9). VAMP7 also appears to have a key role in T-cell activation by facilitating the recruitment of vesicular Lat to the immunological synapse (10). The VAMP7 protein interacts with ATG16L, a component of the ATG5-ATG12 complex, and regulates autophagosome maturation through homotypic fusion of ATG16L1 vesicles (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (1,2). The protein has an amino-terminal H1 domain followed by an H2 SNARE domain and a carboxy-terminal membrane anchor (3). Syntaxin 6 protein is localized to the trans-Golgi and within endosomes and regulates membrane trafficking by partnering with a variety of other SNARE proteins (3-5). Depending on cell type and SNARE parter, syntaxin 6 is involved in the regulation of GLUT4 trafficking, neutrophil exocytosis and granule secretion (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).