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Katalogové číslo: (BOSSBS-5935R-A488)
Dodavatel: Bioss
Popis: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-5104R-HRP)
Dodavatel: Bioss
Popis: Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates.
Měrná jednotka: 1 * 100 µl


Dodavatel: Biotium
Popis: 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.

Katalogové číslo: (ENZOBMLP3160500)
Dodavatel: ENZO LIFE SCIENCES
Popis: PTP substrate
Měrná jednotka: 1 * 0,5 mg


Katalogové číslo: (BOSSBS-1135R-CY5.5)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1135R-A647)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1135R-A488)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1135R-A750)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (ENZOALX260050M005)
Dodavatel: ENZO LIFE SCIENCES
Popis: Granzyme B substrate
Měrná jednotka: 1 * 5 mg


Katalogové číslo: (ENZOALX162004M001)
Dodavatel: ENZO LIFE SCIENCES
Popis: Excellent PKC substrate
Měrná jednotka: 1 * 1 mg


Katalogové číslo: (ENZOBMLP3030005)
Dodavatel: ENZO LIFE SCIENCES
Popis: Proteinase substrate
Měrná jednotka: 1 * 5 mg


Katalogové číslo: (BOSSBS-5935R)
Dodavatel: Bioss
Popis: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-9515R-FITC)
Dodavatel: Bioss
Popis: Catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure.Defects in CTH are the cause of cystathioninuria (CSTNU). It is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.
Měrná jednotka: 1 * 100 µl


Dodavatel: Apollo Scientific
Popis: Substrate for the histochemical demonstration of acid and alkaline phosphatase

Katalogové číslo: (786-320)
Dodavatel: G-Biosciences
Popis: The Fluoro™ Protease Assay Kit is designed for the quantitative determination of proteases present in a protein sample. The assay uses fluorescein isothiocyanate (FITC)-labelled casein as a general protease substrate. The fluorescein label on the FITC-casein is highly quenched. When the proteases present in the sample of interest digest the FITC-casein substrate into smaller peptides, the quenching of the fluorescence label is relieved and the fluorescence of the substrate is increased. The fluorescence of the FITC-labeled peptide is measured with excitation at 485 nm and emission at 530 nm to determine protease activity. The kit detects picogram level of proteases present in the sample.
Měrná jednotka: 1 * 1 KIT


Dodavatel: Apollo Scientific
Popis: A substrate of hexokinase isozymes.

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Omezené množství produktu na skladě. Zboží může být k dispozici v jiném skladě poblíž vašeho sídla. Přesvědčte se, že jste přihlášení na stránky, abyste mohli vidět dostupné položky na skladě. Pokud je stále zobrazeno call a potřebujete asistenci, volejte na číslo 321 570 321.
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