3-Cyano-2,6-difluorobenzoic+acid
Lieferant:
COMBI-BLOCKS
Beschreibung:
2,6-Dimethoxy-3-pyridinboronsäurepinakolester
Lieferant:
COMBI-BLOCKS
Beschreibung:
2,6-Dichlor-3-nitrophenylboronsäure
Artikel-Nr:
(COBBPN-8736-1G)
Lieferant:
COMBI-BLOCKS
Hersteller-Artikelnummer::
PN-8736-1G
Lokale Artikelnummer::
COBBPN-8736-1G
Beschreibung:
2,6-Difluor-4-formylphenylboronsäurepinakolester
VE:
1 * 1 g
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Artikel-Nr:
(COBBPN-5680-1G)
Lieferant:
COMBI-BLOCKS
Hersteller-Artikelnummer::
PN-5680-1G
Lokale Artikelnummer::
COBBPN-5680-1G
Beschreibung:
2,6-Dimethoxy-4-pyridinboronsäurepinakolester
VE:
1 * 1 g
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Lieferant:
FLUOROCHEM
Beschreibung:
2,6-Bis(trifluormethyl)benzoesäure
Artikel-Nr:
(01324-1L)
Lieferant:
Honeywell Chemicals
Hersteller-Artikelnummer::
01324-1L
Lokale Artikelnummer::
HONC01324-1L
Beschreibung:
High purity solvents for speciation analysis by LC-ICP-MS. Rigorous purification procedures followed by UV spectroscopy, IC, and ICP-MS testing to assure high chemical purity and high UV transmittance. The blank values for metal traces in these solvents are in the ppb range or lower.
VE:
1 * 1 L
Lieferant:
COMBI-BLOCKS
Beschreibung:
2,6-Difluor-3-(2'-fluorbenzyloxy)phenylboronsäure
Lieferant:
Sigma-Aldrich
Beschreibung:
2,6-Bis(trifluormethyl)benzoesäure, Sigma-Aldrich®
Lieferant:
COMBI-BLOCKS
Beschreibung:
2,6-Difluor-3,5-dipyridinboronsäurepinakolester
Artikel-Nr:
(SIAL541079-5G)
Lieferant:
Sigma-Aldrich
Hersteller-Artikelnummer::
541079-5G
Lokale Artikelnummer::
SIAL541079-5G
Beschreibung:
Ethyl-2,6-dihydroxybenzoat, Sigma-Aldrich®
VE:
1 * 5 g
Lieferant:
Thermo Scientific
Beschreibung:
2,6-Dihydroxy-9,10-anthrachinon
Artikel-Nr:
(SIALA89502-5G)
Lieferant:
Sigma-Aldrich
Hersteller-Artikelnummer::
A89502-5G
Lokale Artikelnummer::
SIALA89502-5G
Beschreibung:
2,6-Dihydroxy-9,10-anthrachinon, Sigma-Aldrich®
VE:
1 * 5 g
Artikel-Nr:
(BOSSBS-1135R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-HRP
Lokale Artikelnummer::
BOSSBS-1135R-HRP
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-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-A555
Lokale Artikelnummer::
BOSSBS-1135R-A555
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-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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