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1-(4-Chlorophenyl)-1-methylethylamine
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1-(4-Chlorophenyl)-1-methylethylamine
Lieferant:
Bernd Kraft
Beschreibung:
Calciumhydroxid, reinst
Lieferant:
Honeywell Chemicals
Beschreibung:
Calciumhydroxid ≥96%, Puriss. p.a. Reag. Ph. Eur., Fluka™
Lieferant:
Alfa Aesar
Beschreibung:
Hydroxylapatit, schnellfliessend
Artikel-Nr:
(91220.180)
Lieferant:
VWR Chemicals
Lokale Artikelnummer::
VWRC91220.180
Beschreibung:
25 components: Ca 1000 ug/ml, Fe 1000 ug/ml, K 1000 ug/ml, Mg 1000 ug/ml, Na 1000 ug/ml, Ag 10 ug/ml, Al 10 ug/ml, As 10 ug/ml, Ba 10 ug/ml, Be 10 ug/ml, Cd 10 ug/ml, Co 10 ug/ml, Cr 10 ug/ml, Cu 10 ug/ml, Mn 10 ug/ml, Mo 10 ug/ml, Ni 10 ug/ml, Pb 10 ug/ml, Sb 10 ug/ml, Se 10 ug/ml, Tl 10 ug/ml, V 10 ug/ml, Zn 10 ug/ml, Th 10 ug/ml, U 10 ug/ml in 10% HNO₃
VE:
1 * 100 mL
Artikel-Nr:
(BOSSBS-12886R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12886R-A750
Lokale Artikelnummer::
BOSSBS-12886R-A750
Beschreibung:
Cadherins comprise a family of Ca²⁺-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Members of this family of adhesion proteins include rat cadherin K (and its human homolog, cadherin-6), R-cadherin, B-cadherin, E/P cadherin and cadherin-5. The classical cadherins, E-, N- and P-cadherin, consist of large extracellular domains characterised by a series of five homologous NH2 terminal repeats. The most distal of these cadherins is thought to be responsible for binding specificity, transmembrane domains and carboxy terminal intracellular domains. The relatively short intracellular domains interact with a variety of cytoplasmic proteins, such as -catenin, to regulate cadherin function.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13633R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13633R-A555
Lokale Artikelnummer::
BOSSBS-13633R-A555
Beschreibung:
The downstream of kinase family (Dok1-7) are members of a class of “docking†proteins that include the tyrosine kinase substrates IRS-1 and Cas, which contain multiple tyrosine residues and putative SH2 binding sites. Based on their similarities, the Dok family of proteins can be divided into three subgroups: Dok-1/2/3, Dok-4/5/6 and Dok-7. Through its interaction with muscle-specific receptor kinase (MuSK), Dok-7 is crucial for neuromuscular synaptogenesis and for MuSK activation. Mice lacking Dok-7 do not form neuromuscular synapses nor acetylcholine receptor clusters. Mutations in the Dok-7 gene can cause congenital myasthenic syndromes (CMA) — recessively inherited disorders characterized by muscle weakness.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11196R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11196R-A750
Lokale Artikelnummer::
BOSSBS-11196R-A750
Beschreibung:
The cadherins are a family of Ca²⁺ dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino terminus, which is characterised by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including catenin b, to regulate cadherin function. R-cadherin (for retinal-cadherin, also designated cadherin-4), which was first identified in the retina of chicken, has been shown to be involved in the development of striated muscle and potentially epithelia in addition to its involvement in retinal development.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11196R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11196R-A647
Lokale Artikelnummer::
BOSSBS-11196R-A647
Beschreibung:
The cadherins are a family of Ca++-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including catenin b, to regulate cadherin function. R-cadherin (for retinal-cadherin, also designated cadherin-4), which was first identified in the retina of chicken, has been shown to be involved in the development of striated muscle and potentially epithelia in addition to its involvement in retinal development.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12161R-A488)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12161R-A488
Lokale Artikelnummer::
BOSSBS-12161R-A488
Beschreibung:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-signaling between cAMP and Ca(+2)-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
VE:
1 * 100 µl
Lieferant:
G-Biosciences
Beschreibung:
Concanavalin A (Con A) agarose consists of Con A coupled to 6% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from <i>Canavalia ensiformis</i> (jack bean). It is used for the purification of glycoproteins, polysaccharides and glycolipids as it binds molecules containing α-D-mannopyranosyl, α-D-glucopyranosyl and sterically related residues. It has also be used in other application areas including purification of enzyme-antibody conjugates, purification of IgM and separation of membrane vesicles. As stated above, it is a metalloprotein and to maintain its binding characteristics the presence of both Mn²⁺ and Ca²⁺ is essential. Each subunit of Con A utilises one calcium and one manganese ion and these cations can be removed under acidic conditions abolishing the carbohydrate-binding activity.
Artikel-Nr:
(BOSSBS-12161R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12161R-FITC
Lokale Artikelnummer::
BOSSBS-12161R-FITC
Beschreibung:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-signaling between cAMP and Ca(+2)-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12161R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12161R-A555
Lokale Artikelnummer::
BOSSBS-12161R-A555
Beschreibung:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-signaling between cAMP and Ca(+2)-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11196R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11196R-A680
Lokale Artikelnummer::
BOSSBS-11196R-A680
Beschreibung:
The cadherins are a family of Ca²⁺ dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino terminus, which is characterised by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including catenin b, to regulate cadherin function. R-cadherin (for retinal-cadherin, also designated cadherin-4), which was first identified in the retina of chicken, has been shown to be involved in the development of striated muscle and potentially epithelia in addition to its involvement in retinal development.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-7115R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7115R-HRP
Lokale Artikelnummer::
BOSSBS-7115R-HRP
Beschreibung:
MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-7115R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7115R-A647
Lokale Artikelnummer::
BOSSBS-7115R-A647
Beschreibung:
MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-7115R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7115R-A680
Lokale Artikelnummer::
BOSSBS-7115R-A680
Beschreibung:
MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected <i>in vitro</i> with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterised early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.
VE:
1 * 100 µl
Preis auf Anfrage
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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