You Searched For: CENTA\\u2122+\\u03B2-Lactamase+Substrate

Supplier: Thermo Fisher Scientific

Description: Strontium titanate substrate 5x5x1 mm, polished one side 100 orientation

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Catalog Number: (40277.KT)

Supplier: Thermo Fisher Scientific

Description: Strontium titanate substrate 10x10x0.5 mm, polished one side 111 orientation

UOM: 1 * 1 items

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Supplier: Thermo Fisher Scientific

Description: 3,3',5,5'-Tetramethylbenzidine (TMB) EASY, liquid substrate

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Catalog Number: (ENZOBMLP2330001)

Supplier: ENZO LIFE SCIENCES

Description: AMPK substrate

UOM: 1 * 1 mg

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Catalog Number: (ENZOBMLP1570001)

Supplier: ENZO LIFE SCIENCES

Description: This peptide sequence, EFpYAEVGRSPPDPAK, was selected by phage display analysis for optimal Shp-1 and Shp-2 phosphatase activities.

UOM: 1 * 1 mg

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Catalog Number: (CAYM601010-1)

Supplier: Cayman Chemical

Description: For the measurement of NET-derived neutrophil elastase.

UOM: 1 * 1 items

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Catalog Number: (ENZOBMLP1000001)

Supplier: ENZO LIFE SCIENCES

Description: This sequence, KSDGGVKKRKSSSS, is from Ca2+/calmodulin-dependent protein kinase II-γ (345-358).

UOM: 1 * 1 mg

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Supplier: Thermo Fisher Scientific

Description: Magnesium oxide substrate 10x10x0.5mm, polished one side 110 orientation

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Catalog Number: (41436.KT)

Supplier: Thermo Fisher Scientific

Description: Magnesium oxide substrate 10x10x0.5mm, polished two sides 100 orientation

UOM: 1 * 1 items

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Supplier: Merck

Description: Immobilon® Western HRP substrates are compatible with both PVDF and nitrocellulose membranes, as well as all commonly used buffers and blocking reagents.

Catalog Number: (CAYM700420-96)

Supplier: Cayman Chemical

Description: A kit for measuring ascorbate.

UOM: 1 * 1 items

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Supplier: Biotium

Description: NucView® 488 caspase-3 substrate is a novel cell membrane-permeable fluorogenic caspase substrate designed for detecting caspase-3 activity within live cells in real time.

Catalog Number: (BOSSBS-1135R-CY5.5)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1135R-A647)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1135R-A488)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1135R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale