3573 Results for: "4-[(2-Tetrahydropyranyl)oxy]phenol"

Supplier: MACHEREY-NAGEL

Photometric test kit for the determination of pH in water samples.

Supplier: Brand

PP or PS, non sterile. Designed for a wide range of applications, such as high throughput screening, cell and tissue cultures, serial dilutions, reagent transfer, and sample storage down to −80 °C (PP) or −20 °C (PS). Deep well plates are manufactured in standard ANSI/SLAS 1 and 4 format and are stackable for easy storage.

Supplier: Bioss

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.

Supplier: Thermo Fisher Scientific

Employ the most widely used MS phase in gas chromatography with the 5% phenyl phase Thermo Scientific TraceGOLD TG-5MS GC Column. These columns have exceptionally low bleed for optimal signal-to-noise ratio, sensitivity and MS integrity.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: HyClone products (Cytiva)

HyClone™ ActiPro™ cell culture media has been formulated to provide high yields of recombinant proteins in bioprocesses using Chinese hamster ovary (CHO) cell lines. The cultured medium is chemically defined, animal-derived component-free (ADCF), and optimized for high-yield protein expression and production in batch or CHO fed-batch cell culture processes.

Supplier: PROVITRO

The supplement kit designed for cultivating human smooth muscle cells (HSMC) provides an optimised formulation for promoting growth and maintaining the health of these cells. Upon adding the components of the supplement kit to a 500 ml basal medium, a specialised environment is created to support the culture of HSMCs. The formulation is specifically tailored for the initial seeding of 4000 cells per square centimeter, aiming to achieve confluence at approximately 90%. Due to the possibility of reduced proliferative activity we recommend to use the antibiotic supplement for freshly isolated cells only. All components are subjected to rigorous biological assays. Each batch is specifically examined for the proliferating characteristics of human smooth muscle cells (HSMC). The cells cultured in the smooth muscle cell growth medium undergo thorough assessments, including examination of their morphology, adherence rate, colony-forming efficiency, and population doubling time.

Supplier: Merck

All Spectroquant® test kits can be used with the Prove range of spectrophotometers and Nova 60/60A instruments. Tests can be used not only on photometers and spectrophotometer from Merck, but also on photometers and spectrophotometers from other suppliers (programming details available on request).

Supplier: MP Biomedicals

Quick Isolation of genomic DNA from soil using magnetic beads technology.

Supplier: MP Biomedicals

The MagBeads FastDNA Kit for Feces allows thorough sample lysis and quick isolation of DNA from fecal samples. It is using magnetic beads with high DNA binding capacity for extraction of high yields of pure DNA. This is done manually using a magnetic rack or adapted to automated instruments for high throughput processing.

Supplier: VELP SCIENTIFIC

Filter for oxidation chamber for OXITEST 1 * 1 items

Supplier: Merck

All Spectroquant® test kits can be used with the Prove range of spectrophotometers and Nova 60/60A instruments. Tests can be used not only on photometers and spectrophotometer from Merck, but also on photometers and spectrophotometers from other suppliers (programming details available on request). Spectroquant® cell test kits.

Supplier: Merck

PK12 10ML CLEAR MICRO REACTION VESSEL W/ HOLE CAP 1 * 12 items

Supplier: DWK Life Sciences

CAP PP 38-430 WITH PTFE/SI LINER 1 * 48 items

Supplier: Merck

4-OXO-TEMPO, FREE RADICAL 1 * 1 g

Supplier: Merck

2-(2-THIAZOLYLAZO)-P-CRESOL, 97% 1 * 1 g

Supplier: LGC Standards PROMOCHEM

BISOPROLOL ESTER 1 * 100 mg

Supplier: Lovibond

PHENOLRED SOLUTION 1 * 100 mL

Supplier: Merck

(+/-)-DOI HYDROCHLORIDE (+-)-2,5-DIMETHO XY-4- 1 * 500 mg

Supplier: Merck

4-Amino-2-iodophenol 1 * 1 g

Supplier: Lovibond

PHENOLRED PHOTOMETER TABLETS 1 * 500 Tablet

Supplier: Merck

4-Hexylphenol 1 * 25 g

Supplier: CHEMetrics

0 to 1, 0 to 12 ppm 1 * 1 KIT