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Image non disponible-NOVUNB120-11193

Anti-VINC Mouse monoclonal antibody

Numéro de catalogue: (NOVUNB120-11193)
Fournisseur: Novus Biologicals
Description: The Vinculin Antibody (VIN-11-5) from Novus Biologicals is a mouse monoclonal antibody to Vinculin. This antibody reacts with human, mouse, bovine, chicken. The Vinculin Antibody (VIN-11-5) has been validated for the following applications: Western Blot, Immunocytochemistry / Immunofluorescence, Microarray.
UOM: 1 * 0,1 mL
Image non disponible-ROCKMB-045

SSC buffer, 20X concentrate, pH 7,0

Numéro de catalogue: (ROCKMB-045)
Fournisseur: Rockland Immunochemicals
Description: Saline-sodium citrate (SSC) buffer is most commonly used as a buffer for the hybridisation process and washing in experiments where spcies of nucleic or ribonucleic acid are to be matched to complimentary sequences (such as Southern and Nouthern blotting, <i>in situ</i> hybridisation, or DNA microarrays). SSC is used to help control the stringency of hybridisation in these steps.
UOM: 1 * 1 L
Image non disponible-NOVUNB120-10454

Anti-CASP11 Rat monoclonal antibody

Numéro de catalogue: (NOVUNB120-10454)
Fournisseur: Novus Biologicals
Description: The Caspase-11 Antibody (17D9) from Novus Biologicals is a rat monoclonal antibody to Caspase-11. This antibody reacts with human, mouse. The Caspase-11 Antibody (17D9) has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunoprecipitation, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen, Microarray.
UOM: 1 * 0,1 mL
Image non disponible-40028.

CF® Dye dCTP conjugates

Fournisseur: Biotium
Description: CF® dye-dCTP can be used to synthesise probes for in situ hybridisation, microarray, or to synthesise labelled DNA probes for in situ hybridisation and nucleic acid blotting applications.

Image non disponible-BOSSBS-1135R-CY5

Anti-SRC Rabbit Polyclonal Antibody (Cy5®)

Numéro de catalogue: (BOSSBS-1135R-CY5)
Fournisseur: 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
Image non disponible-40063.

Fluorescein-12-dUTP, poudre lyophilisée

Numéro de catalogue: (40063.)
Fournisseur: Biotium
Description: Fluorescein-12-dUTP can be used to synthesize fluorecently labeled DNA probes for in-situ hybridization, microarray or blotting techniques.
UOM: 1 * 25 Nmo
Image non disponible-IMMRIR2937

Anti-IgG (H+L) F(ab)'2 Goat Polyclonal Antibody (APC (Allophycocyanin))

Numéro de catalogue: (IMMRIR2937)
Fournisseur: ImmunoReagents
Description: The ImmunoReagents' Allophycocyanin (APC) is an intensely bright phycobiliprotein isolated from red algae that exhibits far-red fluorescence with high quantum yields. It is excited by laser lines at 594 and 633 nm, with an absorbance maximum at 650 nm and a fluorescence emission peak at 660 nm. APC is a large molecule that is chemically crosslinked to use in fluorescence-based detection, primarily for flow cytometry, microarray assays, ELISAs, and other applications that require high sensitivity but not photostability.
UOM: 1 * 0,5 mL
Image non disponible-40006.

Dye conjugates dUTP CF®

Fournisseur: Biotium
Description: CF® dye-dUTP can be used for TUNEL assay, microarray, or to synthesize labelled DNA probes for <i>in situ</i> hybridisation and nucleic acid blotting applications.

Image non disponible-R1034-02

Kit E-Z 96® Total RNA

Fournisseur: OMEGA BIO-TEK
Description: Le kit E-Z 96® Total RNA est conçu pour l'isolement de l'ARN cellulaire total provenant d'au plus 5×10⁶ cellules en culture ou tissus mous. Ce kit peut traiter des échantillons simples ou multiples en moins de 60 minutes. Comme il utilise la technologie des plaques de silice HiBind®, les extractions au phénol/chloroforme, l'ultracentrifugation en gradient de CsCl et la précipitation à l'isopropanol ou LiCl sont superflues. Les échantillons sont lysés dans un tampon de lyse dénaturant qui désactive les RNases. Les conditions de liaison sont ajustées et le lysat est transféré vers une plaque de 96 puits HiBind® RNA où l'ARN est purifié par trois étapes de lavage. L'ARN de grande qualité est élué dans de l'eau exempte de RNase. L'ARN purifié à l'aide de la méthode E-Z 96® Total RNA est prêt à l'emploi pour des applications telles que la RT-PCR, la qPCR, le DD, les microéchantillons, ainsi que pour d'autres applications en aval.

MSMD

Image non disponible-BOSSBS-1135R-A680

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 680)

Numéro de catalogue: (BOSSBS-1135R-A680)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-A488

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Numéro de catalogue: (BOSSBS-1135R-A488)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-CY5.5

Anti-SRC Rabbit Polyclonal Antibody (Cy5.5®)

Numéro de catalogue: (BOSSBS-1135R-CY5.5)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-A647

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Numéro de catalogue: (BOSSBS-1135R-A647)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-A750

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Numéro de catalogue: (BOSSBS-1135R-A750)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-A350

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Numéro de catalogue: (BOSSBS-1135R-A350)
Fournisseur: 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
Image non disponible-BOSSBS-1135R-CY3

Anti-SRC Rabbit Polyclonal Antibody (Cy3®)

Numéro de catalogue: (BOSSBS-1135R-CY3)
Fournisseur: 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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