Methyl+2,3-diamino-6-fluorobenzoate
Lieferant:
APOLLO SCIENTIFIC
Beschreibung:
Pyridoxine-[2H3].HCl
Artikel-Nr:
(17934-50ML)
Lieferant:
Sigma-Aldrich
Hersteller-Artikelnummer::
17934-50ML
Lokale Artikelnummer::
SUPL17934-50ML
Beschreibung:
Chlorwasserstoff 1.25 mol/l in Ethanol, Supelco®
VE:
1 * 50 mL
Lieferant:
Sigma-Aldrich
Beschreibung:
Chlorwasserstoff 1.25 mol/l in Methanol, Supelco®
Lieferant:
PanReac AppliChem
Beschreibung:
TRIS HCl (Tris(hydroxymethyl)aminomethan Hydrochlorid)
Artikel-Nr:
(PRSI28-997)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
28-997
Lokale Artikelnummer::
PRSI28-997
Beschreibung:
BRD7 is an activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. It induces dephosphorylation of GSK3B at 'Tyr-216'.
VE:
1 * 50 µG
Artikel-Nr:
(8.24456.0500)
Lieferant:
Merck
Hersteller-Artikelnummer::
8.24456.0500
Lokale Artikelnummer::
MERC8.24456.0500
Beschreibung:
(2S,4R)-(-)-Ethyl-4-hydroxy-2-pyrrolidincarboxylate hydrochloride zur Synthese, Sigma-Aldrich®
VE:
1 * 500 mg
Artikel-Nr:
(APOSOR963265-25G)
Lieferant:
APOLLO SCIENTIFIC
Hersteller-Artikelnummer::
OR963265-25G
Lokale Artikelnummer::
APOSOR963265-25G
Beschreibung:
N-Boc-1,4-diaminobutane-HCl
VE:
1 * 25 g
Artikel-Nr:
(PRSI79-648)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
79-648
Lokale Artikelnummer::
PRSI79-648
Beschreibung:
Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates ERK1 and ERK2 MAP kinases.
VE:
1 * 100 µG
Artikel-Nr:
(BOSSBS-1764R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1764R-HRP
Lokale Artikelnummer::
BOSSBS-1764R-HRP
Beschreibung:
Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium.
VE:
1 * 100 µl
Lieferant:
Simport Scientific
Beschreibung:
These MultiRack™ Jr. are ideal for use in incubators, refrigerators, freezers, under lab hoods and om benchtops.
Artikel-Nr:
(PRSI92-001)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
92-001
Lokale Artikelnummer::
PRSI92-001
Beschreibung:
As an adaptor protein, Growth Factor Receptor-Bound Protein 2 (GRB2) is involved in siganl transduction and consists of a central SH2 domain flanked by two SH3 domains. GRB2 associates with activated Tyr-phosphorylated EGF receptor/EGFR and PDGF receptors via its SH2 domain, stimulating GTP binding to Ras, which in turn activates MAPK and other signaling pathway.It also associates to other cellular Tyr-phosphorylated proteins such as SIT1, IRS1, IRS4, SHC and LNK. probably via the concerted action of both its SH2 and SH3 domains.
VE:
1 * 50 µG
Artikel-Nr:
(PRSI79-195)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
79-195
Lokale Artikelnummer::
PRSI79-195
Beschreibung:
Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates ERK1 and ERK2 MAP kinases.
VE:
1 * 100 µG
Artikel-Nr:
(BOSSBS-1135R-A488)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-A488
Lokale Artikelnummer::
BOSSBS-1135R-A488
Beschreibung:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1135R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-A750
Lokale Artikelnummer::
BOSSBS-1135R-A750
Beschreibung:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labelling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr --> Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1135R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-A647
Lokale Artikelnummer::
BOSSBS-1135R-A647
Beschreibung:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1135R-CY5.5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-CY5.5
Lokale Artikelnummer::
BOSSBS-1135R-CY5.5
Beschreibung:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
VE:
1 * 100 µl
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