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3,4-Dimethoxyphenylborons\\u00E4urepinakolester
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3,4-Dimethoxyphenylborons\\u00E4urepinakolester
Artikel-Nr:
(COBBBB-2592-10G)
Lieferant:
COMBI-BLOCKS
Hersteller-Artikelnummer::
BB-2592-10G
Lokale Artikelnummer::
COBBBB-2592-10G
Beschreibung:
2,6-DIMETHOXYPHENYLBORONIC ACID 1 * 10 g
VE:
1 * 10 g
 This is a MarketSource item. Additional charges may apply
Artikel-Nr:
(APOSOR89766-10MG)
Lieferant:
APOLLO SCIENTIFIC
Hersteller-Artikelnummer::
OR89766-10MG
Lokale Artikelnummer::
APOSOR89766-10MG
Beschreibung:
(R)-2-((6-(3-((3-(2-cyanobenzyl)-1-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)piperidin-1-yl)-3-methyl-2,4-dioxo-3,4-di hydropyrimidin-1(2H)-yl)methyl)benzonitrile 10mg pack 1 * 10 mg
VE:
1 * 10 mg
New Product
Artikel-Nr:
(AMBDA471853-25G)
Lieferant:
AMBEED
Hersteller-Artikelnummer::
A471853-25G
Lokale Artikelnummer::
AMBDA471853-25G
Beschreibung:
2,6-DIMETHOXYPHENYLBORONIC ACID 1 * 25 g
VE:
1 * 25 g
This is a MarketSource item. Additional charges may apply
Artikel-Nr:
(PRSI92-281)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
92-281
Lokale Artikelnummer::
PRSI92-281
Beschreibung:
Mouse Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases.Mouse Shh is synthesised as a 437 aa precursor that contains a 24 aa signal sequence and a 413 aa mature region. The mature region is autocatalytically processed into a nonglycosylated, 20 kDa, 174 aa Nterminal fragment (ShhN), and a catalyticprocessing,glycosylated, 34 kDa, 239 aa Cterminal fragment. The 20 kDa ShhN fragment is the core of the active hedgehog molecule. Mouse ShhN is 99%, 98%, and 100% aa identical to human, rat and gerbil ShhN, respectively.
VE:
1 * 50 µG
Artikel-Nr:
(PRSI92-284)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
92-284
Lokale Artikelnummer::
PRSI92-284
Beschreibung:
Mouse Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases.Mouse Shh is synthesised as a 437 aa precursor that contains a 24 aa signal sequence and a 413 aa mature region. The mature region is autocatalytically processed into a nonglycosylated, 20 kDa, 174 aa Nterminal fragment (ShhN), and a catalyticprocessing,glycosylated, 34 kDa, 239 aa Cterminal fragment. The 20 kDa ShhN fragment is the core of the active hedgehog molecule. Mouse ShhN is 99%, 98%, and 100% aa identical to human, rat and gerbil ShhN, respectively.
VE:
1 * 50 µG
Artikel-Nr:
(PRSI50-266)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
50-266
Lokale Artikelnummer::
PRSI50-266
Beschreibung:
Nop1p was originally identified as a nucleolar protein of bakers yeast, Saccharomyces cerevisiae. The Nop1p protein is 327 amino acids in size (34.5 kDa), is essential for yeast viability, and is localized in the nucleoli. The systematic name for S. cerevisiae Nop1 is YDL014W, and it is now known to be part of the small subunit processome complex, involved in the processing of pre-18S ribosomal RNA. Nop1p is the yeast homologue of a protein found in all eukaryotes and archea generally called fibrillarin. Fibrillarin/Nop1p is extraordinarily conserved, so that the yeast and human proteins are 67% identical, and the human protein can functionally replace the yeast protein. Patients with the autoimmune disease scleroderma often have strong circulating autoantibodies to a ~34 kDa protein which was subsequently found to be fibrillarin. Recent studies show that knock-out of the fibrillarin gene in mice results in embryonic lethality, although mice with only one functional fibrillarin/Nop1p gene were viable. This antibody is becoming widely used as a convenient marker for nucleoli in a wide variety of species (e.g. 4-6).
VE:
1 * 100 µl
Artikel-Nr:
(PRSI90-395)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
90-395
Lokale Artikelnummer::
PRSI90-395
Beschreibung:
CD40 Ligand (CD40L), renamed TNFSF5 but now also known as CD154, TRAP and gp39, is a 34-39kDa type II transmembrane glycoprotein that belongs to the TNF superfamily. As with other TNF superfamily members, CD40L will exist as a trimer, both as a membrane bound and soluble form. Multiple mutations and alternate splice forms of CD40L exist, often associated with pathology and leading to truncated or nontrimerizable forms of CD40L. CD40L binds to both CD40 and to integrin alphaIIbbeta3 (CD41). In the cell membrane, it also associates with a unique splice variant of CD28 (CD28i) that may facilitate CD40L signal transduction. CD40L is expressed by monocytes, NK cells, mast cells, basophils, smooth muscle cells, endothelial cells, dendritic cells,activated and resting B cells, plus activated platelets and CD4+ T cells. CD40L ligation of CD40 on dendritic cells (DC) initiates DC maturation and differentiation. CD40L signalling into naive B cells promotes germinal center formation and isotope switching. CD40-CD40L seems to bridge innate and adaptive immune signals.
VE:
1 * 50 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
Artikel-Nr:
(BOSSBS-1135R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-A680
Lokale Artikelnummer::
BOSSBS-1135R-A680
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-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-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-CY3
Lokale Artikelnummer::
BOSSBS-1135R-CY3
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-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1135R-FITC
Lokale Artikelnummer::
BOSSBS-1135R-FITC
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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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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