7567 Results for: "4-(Methylamino)phenol+sulphate"

Supplier: MP Biomedicals

Quick and convenient purification of total RNA from animal tissues, plant tissues and tissue cultures using spin column technology.

Supplier: 3M Food Safety

The 3M™ Quick Swab is a ready-to-use environmental swab system consisting of a five inch, rayon-tipped swab containing Letheen neutralising buffer to facilitate recovery of bacteria.

Supplier: Thermo Fisher Scientific

These desalting columns are ready-to-use, disposable, gel filtration columns for separating proteins and other macromolecules from low molecular weight buffer salts and reagents.

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: MP Biomedicals

Storage: Store at room temperature (15-30 °C)
L-Tyrosine is one of the three aromatic amino acids, and is formed from the hydroxylation of phenylalanine.
L-Tyrosine is used in cell culture media and is a component of MEM amino acids solution. L-Tyrosine has been used in a cell culture study of the amino acid transport system b0,+ in epithelial cells isolated from chicken jejunum.

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: Biotium

6X DNA loading buffer that includes ultra-sensitive, non-toxic GelRed® dye.

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: 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: OMEGA BIO-TEK

Isolate up to 25 µg plasmid DNA from 1 to 5 ml bacterial cultures using mini spin columns.

Supplier: OMEGA BIO-TEK

Isolate total RNA from cells or soft tissues using spin column.

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: VWR Chemicals

Easy to use method for isolation up to 100 µg of total RNA from cultured eukaryotic cells and soft tissues <1×10⁷ cells or 30 mg tissue.

Supplier: OMEGA BIO-TEK

Isolate up to 25 µg plasmid DNA from 1 to 5 ml bacterial cultures using mini spin columns.

Supplier: MP Biomedicals

Applications
Taurocholic Acid Sodium Salt is an anionic detergent used for protein solubilization.
Product Description
Taurocholic Acid Sodium Salt is the conjugation product of cholic acid with taurine and the principal constituent of the bile of carnivorous animals.
Biochem/physiol Actions
Non-sulfated bile salt, physiological transport substrate for the bile salt export pump/sister of Pgp (BSEP/spgp), Na(+)/taurocholate cotransporter (NTCP) and MRP3 into the hepatic carnalicular.

Melting Point: 230 °C (decomposes)(Lit.)
Presentation: White Powder
Format: Powder
pH: 6 - 7.5(1% aq soln)
Aggregation Number: 4
Critical Micelle Concentration (CMC): 3-11 mM
Heavy Metals: =20 ppm
Loss on Drying: =7.0%
NOTES: Sodium Cholate : =3.0%
Solubility: Soluble in water (100 mg/mL).
Storage & Handling: Store at Room Temperature (15-30 °C).

Supplier: VWR Chemicals

Isolate up to 40 to 70 µg of high quality plasmid DNA from up to 15 ml bacterial cultures in 30 minutes or less. Simplified with VWR® peqGold Mini Column II technology into three quick steps: Bind, wash and elute.

Supplier: ENZO LIFE SCIENCES

EPIXTRACT® DNA isolation kit provides a simple method to isolate DNA from plasma, serum, and body fluids.

Supplier: VWR Chemicals

TriFast™ is a complete ready to use reagent for simultaneous isolation of RNA, DNA and proteins from liquid samples, tissue and cells.

Supplier: OMEGA BIO-TEK

By adapting HiBind® technology with 96-well plates, the E-Z 96® Tissue DNA kit provides a high throughput method to purify genomic DNA from whole blood, buccal swabs, mouse tail, rat tail, tissues and animal cells and tissues in a 96-well plate format. Purified DNA is suitable for most downstream applications such as PCR, restriction enzyme digestion, and hybridisation techniques.

Supplier: OMEGA BIO-TEK

The E.Z.N.A.® Forensic DNA Kit is designed to provide a rapid and easy method for the isolation of genomic DNA from forensic samples such as dry blood, buccal swabs, and semen samples for consistent PCR and Southern analysis. This kit can also be used for the preparation of genomic DNA from mouse tail snips, whole blood, buffy coat, serum, and plasma.

Supplier: G-Biosciences

OmniPrep™ for Plant Kit isolates high quality genomic DNA from plant samples, including fresh and frozen plant tissues. If used according to the protocols this kit purifies DNA from 20gm plant tissue.

Supplier: G-Biosciences

OmniPrep™ for Blood Kit isolates high quality genomic DNA from blood samples, including whole blood, buffy coats, packed cells and bone marrow.

Supplier: G-Biosciences

OmniPrep™ for Yeast Kit isolates high quality genomic DNA from yeast. When used according to the recommended protocols, this kit purifies DNA from 300 ml yeast culture.