You Searched For: Fraction+Collectors

Catalog Number: (ROCK600-103-200)

Supplier: Rockland Immunochemicals

Description: Primary Goat Anti-GLUTATHIONE-S-TRANSFERASE (Schistosoma japonicum) IgG Fraction Reacts with Pan

UOM: 1 * 1 mg

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Catalog Number: (BOSSBS-12945R-A647)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12944R-A488)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12944R-A350)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12944R-A750)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca²⁺-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca²⁺ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A350)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12944R-A647)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A555)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12944R-A680)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca²⁺-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca²⁺ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12945R-A750)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca²⁺-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca²⁺ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1882R-A647)

Supplier: Bioss

Description: MRas is a member of the RAS superfamily of GTP-binding proteins which are membrane-anchored, intracellular signal transducers responsible for a variety of normal cellular functions. They are oncogenically activated in a significant fraction of tumors. MRas participates in reorganisation of actin cytoskeleton. It is also involved in focal adhesion and can activate MAPK signalling.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3957R-A350)

Supplier: Bioss

Description: NDUFA10 protein belongs to the complex I 42kDa subunit family. Mammalian complex I is the first enzyme complex in the electron transport chain of mitochondria. It is composed of 45 different subunits. This protein is a component of the hydrophobic protein fraction and has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain.

UOM: 1 * 100 µl

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Catalog Number: (ROCK600-101-200)

Supplier: Rockland Immunochemicals

Description: Primary Goat Anti-GLUTATHIONE-S-TRANSFERASE (Schistosoma japonicum) IgG Fraction Reacts with GST,

UOM: 1 * 1 mg

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Catalog Number: (BOSSBS-1882R-CY7)

Supplier: Bioss

Description: MRas is a member of the RAS superfamily of GTP-binding proteins which are membrane-anchored, intracellular signal transducers responsible for a variety of normal cellular functions. They are oncogenically activated in a significant fraction of tumors. MRas participates in reorganisation of actin cytoskeleton. It is also involved in focal adhesion and can activate MAPK signalling.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4141R)

Supplier: Bioss

Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5522R)

Supplier: Bioss

Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.

UOM: 1 * 100 µl

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