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PDGF receptor tyrosine kinase inhibitor IV ≥97%

Supplier: Ambeed
Description: PDGF receptor tyrosine kinase inhibitor IV ≥97%

New Product

Image Unavailable-76002-482

PDGF receptor tyrosine kinase inhibitor IV ≥99% (by HPLC)

Catalog Number: (76002-482)
Supplier: Enzo Life Sciences
Description: Cell-permeable PDGFR inhibitor with antiproliferative properties.
Product Image-89147-104

Tyrphostin AG 1295 ≥98%

Catalog Number: (89147-104)
Supplier: Enzo Life Sciences
Description: Selective inhibitor of tyrosine kinase in platelet-derived growth factor (PDGF) receptor.
Image Unavailable-89157-822

Tyrphostin B7 ≥99% (by TLC)

Supplier: Enzo Life Sciences
Description: Member of the tyrphostin family of tyrosine kinase inhibitors. Selective inhibitor of the PDGF receptor kinase (IC50=20µM) vs. the EGF receptor kinase (IC50=820µM). Inhibits PDGF-induced mitogenesis in human bone marrow fibroblasts.

Image Unavailable-89158-012

Tyrphostin AG-1296 ≥98% (by TLC)

Supplier: Enzo Life Sciences
Description: A potent inhibitor of PDGF receptor tyrosine kinase (IC50=1 µM). Also inhibits FGF receptor tyrosine kinase and c-kit. Induces apoptosis in a small-cell lung cancer cell line (H526).

Image Unavailable-89157-794

Tyrphostin A9 ≥99% (by HPLC)

Supplier: Enzo Life Sciences
Description: Tyrphostin 9 is a selective inhibitor of the PDGF receptor tyrosine kinase (IC50=1.2 µM). It is also a potent (10 nM) uncoupler of oxidative phosphorylation.

Product Image-76002-076

Bisindolylmaleimide I ≥98% (by TLC)

Supplier: Enzo Life Sciences
Description: Potent and selective protein kinase C inhibitor which has been used effectively in platelets, Swiss 3T3 fibroblasts and macrophages. Inhibitory profile: PKC, IC50=0.02µM (inhibits α, ßI, ßII and γ subtypes with similar potency); PKA, IC50=2.0µM; phosphorylase kinase, IC50=0.7µM; insulin, EGF and PDGF receptor tyrosine kinases are not inhibited at concentrations up to 50µM.

Image Unavailable-10256-594

Anti-SRC Rabbit Polyclonal Antibody

Catalog Number: (10256-594)
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.
Image Unavailable-10254-128

Anti-SRC Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Catalog Number: (10254-128)
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.
Image Unavailable-10254-120

Anti-SRC Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (10254-120)
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.
Image Unavailable-10254-122

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

Catalog Number: (10254-122)
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.
Image Unavailable-10254-126

Anti-SRC Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Catalog Number: (10254-126)
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.
Image Unavailable-10254-118

Anti-SRC Rabbit Polyclonal Antibody (Cy3®)

Catalog Number: (10254-118)
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.
Image Unavailable-10254-124

Anti-SRC Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (10254-124)
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.
Image Unavailable-103481-920

Anti-APS Rabbit Polyclonal Antibody

Catalog Number: (103481-920)
Supplier: Affymetrix, Inc.
Description: PA1-1062 detects APS from mouse samples. PA1-1062 has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~ 84 kDa protein corresponding to APS from recombinant mouse protein and 3T3L1 extracts. The PA1-1062 immunogen is a synthetic peptide corresponding to residues E(605)A T L G R A R A V E N Q Y S(619) from mouse APS. This peptide (Cat. # PEP-246) can be used in neutralization and control experiments. APS (adapter protein with Pleckstrin homology and Src homology 2 domains) a member of the Lnk family, is an adaptor protein that is involved in B-cell signaling, insulin signaling, cytoskeletal reorganization. It is tyrosine phosphorylated by JAK2, KIT and other kinases during B-cell receptor stimulation of many different cytokines, chemokines and leukokines. APS has been shown to inhibit the JAK-STAT pathway in collaboration with c-Cbl. It is located in the cytoplasm in pre-PDGF (platelet derived growth factor) stimulated cells and localizes to the plasma membrane and peripheral regions upon PDGF stimulation.   This protein is expressed in B-cells and mast cells when detected in haematopoietic cell lines yet is also expressed in many different tissues including spleen, prostrate, testis, uterus, small intestine and skeletal muscle.

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Mouse Recombinant PDGF R alpha

Catalog Number: (75791-934)
Supplier: Prosci
Description: Platelet-derived growth factor receptors (PDGFR) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family. The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. PDGFs bind to the protein tyrosine kinase receptors PDGF receptor- alpha and - beta . These two receptor isoforms dimerize upon binding the PDGF dimer, leading to three possible receptor combinations, namely - alpha alpha, - beta beta and - alpha beta . PDGFR alpha and PDGFR beta are members of the class III RTK family. Inappropriate PDGFR alpha and PDGFR beta signaling has been linked to a number of proliferative disorders.
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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 at 1-800-932-5000.
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