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Catalog Number: (ENZOBMLP2290010)
Supplier: ENZO LIFE SCIENCES
Description: Cathepsin substrate
UOM: 1 * 10 mg


Catalog Number: (BOSSBS-9515R)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4210R-FITC)
Supplier: Bioss
Description: Hydrolyzes acyl-CoA thioesters (in vitro). Has a preference for substrates with medium chain length (C1-C14). Inactive towards substrates with C18 or C2 aliphatic chains. Its physiological substrate is not known.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4210R-CY5.5)
Supplier: Bioss
Description: Hydrolyzes acyl-CoA thioesters (in vitro). Has a preference for substrates with medium chain length (C1-C14). Inactive towards substrates with C18 or C2 aliphatic chains. Its physiological substrate is not known.
UOM: 1 * 100 µl


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.

Supplier: ENZO LIFE SCIENCES
Description: Substrate for caspase-1 and -5

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


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


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


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


Supplier: ENZO LIFE SCIENCES
Description: Caspase-9 substrate

Catalog Number: (ENZOALX162004M001)
Supplier: ENZO LIFE SCIENCES
Description: Excellent PKC substrate
UOM: 1 * 1 mg


Catalog Number: (ENZOALX260109M005)
Supplier: ENZO LIFE SCIENCES
Description: Caspase substrate
UOM: 1 * 5 mg


Catalog Number: (BOSSBS-3263R-FITC)
Supplier: Bioss
Description: MARCKS, (Myristoylated Alanine-Rich C Kinase Substrate), is a member of a family of calmodulin binding proteins and is a major substrate for phosphorylation by protein kinase C (PKC). The phosphorylation of Ser152/156 can be used as a measure of PKC activation. Phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3359R-A350)
Supplier: Bioss
Description: MARCKS, (Myristoylated Alanine-Rich C Kinase Substrate), is a member of a family of calmodulin binding proteins and is a major substrate for phosphorylation by protein kinase C (PKC). The phosphorylation of Ser152/156 can be used as a measure of PKC activation. Phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3090R-A647)
Supplier: Bioss
Description: This gene is a proto-oncogene that encodes a RING finger E3 ubiquitin ligase. The encoded protein is one of the enzymes required for targeting substrates for degradation by the proteasome. This protein mediates the transfer of ubiquitin from ubiquitin conjugating enzymes (E2) to specific substrates. This protein also contains an N-terminal phosphotyrosine binding domain that allows it to interact with numerous tyrosine-phosphorylated substrates and target them for proteasome degradation. As such it functions as a negative regulator of many signal transduction pathways. This gene has been found to be mutated or translocated in many cancers including acute myeloid leukaemia. Mutations in this gene are also the cause of Noonan syndrome-like disorder. [provided by RefSeq, Mar 2012]
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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