You Searched For: Fraction+Collectors

Catalog Number: (BOSSBS-12945R-CY3)

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: (BE-404)

Supplier: G-Biosciences

Description: This lab activity is designed to demonstrate the different classes of protein molecules and their classification based on solubility. Students learn fractionation of soluble, insoluble membrane proteins, and cytoskeleton proteins from a tissue sample. The insoluble protein fraction is further fractionated into hydrophilic and hydrophobic membrane proteins. Cell membrane structure and the role of hydrophobic membrane proteins are considered. This lab activity also provides an opportunity to understand characteristics of various classes of detergents and the role of detergents in solubilisation of hydrophobic membrane proteins.

UOM: 1 * 1 KIT

Sale

Catalog Number: (5274.2500)

Supplier: Avantor

Description: n-Hexane, BAKER ANALYZED® Pest_Residual, J.T.Baker®

UOM: 1 * 2,5 L

Certificates Sale

Catalog Number: (BOSSBS-12945R-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

Sale

Catalog Number: (BOSSBS-12945R-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: (24603.290)

Supplier: VWR Chemicals

Description: n-Hexane, anhydrous (max. 0.005% H₂O) ≥97%, AnalaR NORMAPUR® analytical reagent

UOM: 1 * 1 L

MSDS Certificates Sale

Supplier: VWR Chemicals

Description: n-Hexane 95, AnalaR NORMAPUR® Reag. Ph. Eur., ACS zA

MSDS Certificates

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

Sale

Supplier: VWR Chemicals

Description: CRM's - secondary reference materials intended for standardisation of volumetric solutions in accordance with the Pharmacopoeia (Ph. Eur. and USP). These volumetric standards are prepared from high purity salts. Certified mass fraction is determined by classical analysis according to ISO/IEC 17025. Homogeneity and stability studies have been performed according to the requirements of ISO 17034 and ISO Guide 35. All volumetric standards are traceable to SI (NIST or BAM).

MSDS Certificates Sale

Supplier: Biowest

Description: Dog serum is the liquid fraction of whole blood that is collected after the blood is allowed to clot; it is the blood plasma with the fibrinogens removed. Serum includes all proteins not used in blood clotting (coagulation) and all the electrolytes, antibodies, antigens, hormones, and any exogenous substances. Dog serum is used as a blocking agent in immunoassays and controls.

Catalog Number: (BOSSBS-12944R-FITC)

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-FITC)

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-HRP)

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-7694R-A647)

Supplier: Bioss

Description: Key mediator of sodium and chloride reabsorption in this nephron segment, accounting for a significant fraction of renal sodium reabsorption.

UOM: 1 * 100 µl

Sale

Supplier: VWR Chemicals

Description: n-Hexane 99, PESTINORM® Supra Trace Trace_analysis_organic

MSDS

Catalog Number: (BOSSBS-7694R-CY5)

Supplier: Bioss

Description: Key mediator of sodium and chloride reabsorption in this nephron segment, accounting for a significant fraction of renal sodium reabsorption.

UOM: 1 * 100 µl

Sale