3-(tert-Butyldimethylsiloxy)thiophenol
Lieferant:
MP Biomedicals
Beschreibung:
Tris and Tris Hydrochloride have been useful as buffers in a wide variety of biological systems. Uses include pH control<i> in vitro </i>and <i>in vivo</i> for body fluids and in buffering systems for electrophoresis applications.
Artikel-Nr:
(FLUO009735-10G)
Lieferant:
FLUOROCHEM
Hersteller-Artikelnummer::
009735-10G
Lokale Artikelnummer::
FLUO009735-10G
Beschreibung:
5-Amino-3-phenyl-1,2,4-thiadiazol
VE:
1 * 10 g
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Artikel-Nr:
(COBBPY-1754-1G)
Lieferant:
COMBI-BLOCKS
Hersteller-Artikelnummer::
PY-1754-1G
Lokale Artikelnummer::
COBBPY-1754-1G
Beschreibung:
2-Amino-7-bromchinazolin
VE:
1 * 1 g
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Artikel-Nr:
(BOSSBS-11251R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11251R-CY5
Lokale Artikelnummer::
BOSSBS-11251R-CY5
Beschreibung:
Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11251R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11251R-A680
Lokale Artikelnummer::
BOSSBS-11251R-A680
Beschreibung:
Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK Signalling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins. Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterisation suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
VE:
1 * 100 µl
Lieferant:
SIGMA ALDRICH MICROSCOPY
Beschreibung:
Fuchsin basisch, Sigma-Aldrich®
Lieferant:
SIGMA ALDRICH MICROSCOPY
Beschreibung:
Fuchsin basisch, Sigma-Aldrich®
Artikel-Nr:
(SERA30293.01)
Lieferant:
Serva
Hersteller-Artikelnummer::
30293.01
Lokale Artikelnummer::
SERA30293.01
Beschreibung:
Neufuchsin
VE:
1 * 25 g
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Artikel-Nr:
(BOSSBS-11251R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11251R-A647
Lokale Artikelnummer::
BOSSBS-11251R-A647
Beschreibung:
Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11251R-A488)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11251R-A488
Lokale Artikelnummer::
BOSSBS-11251R-A488
Beschreibung:
Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
VE:
1 * 100 µl
Artikel-Nr:
(PRSI7231P)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
7231P
Lokale Artikelnummer::
PRSI7231P
Beschreibung:
13 amino acid peptide near the center of human IL-15.
VE:
1 * 50 µG
Lieferant:
Uptima
Beschreibung:
TRIS HCl (Tris(hydroxymethyl)aminomethan Hydrochlorid)
Artikel-Nr:
(SERA30305.01)
Lieferant:
Serva
Hersteller-Artikelnummer::
30305.01
Lokale Artikelnummer::
SERA30305.01
Beschreibung:
Neutralrot
VE:
1 * 25 g
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Artikel-Nr:
(SIALA52005-25G)
Lieferant:
Sigma-Aldrich
Hersteller-Artikelnummer::
A52005-25G
Lokale Artikelnummer::
SIALA52005-25G
Beschreibung:
2-Amino-4,6-dimethylpyrimidin, Sigma-Aldrich®
VE:
1 * 25 g
Artikel-Nr:
(BOSSBS-11251R-A350)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11251R-A350
Lokale Artikelnummer::
BOSSBS-11251R-A350
Beschreibung:
Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
VE:
1 * 100 µl
Lieferant:
Thermo Scientific
Beschreibung:
7-Amino-4-(trifluormethyl)cumarin
Preis auf Anfrage
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