rabbit anti pret py905 antibodies Search Results


ret  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology ret
Phosphorylation of multiple RTKs in lung cancer cells with MET amplification. ( A ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence (control) or presence of PHA-665752 (500 n M ). Cell lysates were prepared and incubated with an RTK array for determination of the phosphorylation status of each enzyme. Each RTK is spotted in duplicate, and the pairs of dots in each corner of the array are positive controls. The numbered pairs of dots correspond to the indicated phosphorylated (p-) RTKs. ( B ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence or presence of PHA-665752 (PHA, 500 n M ), gefitinib (1 μ M ), lapatinib (1 μ M ), or vandetanib (1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to phosphorylated or total forms of MET, EGFR, <t>HER2,</t> <t>HER3,</t> <t>RET,</t> AKT, ERK, or STAT3 or with those to β -actin (loading control). ( C ) The indicated cell lines were deprived of serum for 24 h and then incubated for 2 h in the absence (Con) or presence of gefitinib (Gef, 1 μ M ), lapatinib (Lap, 1 μ M ), or vandetanib (Van, 1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to the indicated proteins.
Ret, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+pret+py905+antibodies/pmc03171021-19-59-71?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
ret - by Bioz Stars, 2026-07
93/100 stars
  Buy from Supplier

Image Search Results


Phosphorylation of multiple RTKs in lung cancer cells with MET amplification. ( A ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence (control) or presence of PHA-665752 (500 n M ). Cell lysates were prepared and incubated with an RTK array for determination of the phosphorylation status of each enzyme. Each RTK is spotted in duplicate, and the pairs of dots in each corner of the array are positive controls. The numbered pairs of dots correspond to the indicated phosphorylated (p-) RTKs. ( B ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence or presence of PHA-665752 (PHA, 500 n M ), gefitinib (1 μ M ), lapatinib (1 μ M ), or vandetanib (1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to phosphorylated or total forms of MET, EGFR, HER2, HER3, RET, AKT, ERK, or STAT3 or with those to β -actin (loading control). ( C ) The indicated cell lines were deprived of serum for 24 h and then incubated for 2 h in the absence (Con) or presence of gefitinib (Gef, 1 μ M ), lapatinib (Lap, 1 μ M ), or vandetanib (Van, 1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to the indicated proteins.

Journal: British Journal of Cancer

Article Title: Differential roles of trans-phosphorylated EGFR, HER2, HER3, and RET as heterodimerisation partners of MET in lung cancer with MET amplification

doi: 10.1038/bjc.2011.322

Figure Lengend Snippet: Phosphorylation of multiple RTKs in lung cancer cells with MET amplification. ( A ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence (control) or presence of PHA-665752 (500 n M ). Cell lysates were prepared and incubated with an RTK array for determination of the phosphorylation status of each enzyme. Each RTK is spotted in duplicate, and the pairs of dots in each corner of the array are positive controls. The numbered pairs of dots correspond to the indicated phosphorylated (p-) RTKs. ( B ) EBC-1 and H1993 cells were deprived of serum for 24 h and then incubated for 2 h in the absence or presence of PHA-665752 (PHA, 500 n M ), gefitinib (1 μ M ), lapatinib (1 μ M ), or vandetanib (1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to phosphorylated or total forms of MET, EGFR, HER2, HER3, RET, AKT, ERK, or STAT3 or with those to β -actin (loading control). ( C ) The indicated cell lines were deprived of serum for 24 h and then incubated for 2 h in the absence (Con) or presence of gefitinib (Gef, 1 μ M ), lapatinib (Lap, 1 μ M ), or vandetanib (Van, 1 μ M ), after which cell lysates were subjected to immunoblot analysis with antibodies to the indicated proteins.

Article Snippet: Rabbit polyclonal antibodies to phosphorylated human MET (pY1234/pY1235), to phosphorylated EGFR (pY1068), to phosphorylated HER2 (pY1221), to phosphorylated HER3 (pY1289), to phosphorylated RET (pY905), to AKT, to phosphorylated AKT, to signal transducer and activator of transcription 3 (STAT3), to phosphorylated STAT3, and to poly(ADP-ribose) polymerase (PARP) were obtained from Cell Signaling Technology (Danvers, MA, USA); those to HER3, to RET, to extracellular signal-regulated kinase (ERK), and to phosphorylated ERK were from Santa Cruz Biotechnology (Santa Cruz, CA, USA); those to MET were from Zymed (South San Francisco, CA, USA); those to HER2 were from Millipore (Billerica, MA, USA); and those to β -actin were from Sigma.

Techniques: Phospho-proteomics, Amplification, Incubation, Control, Western Blot

Association of MET with EGFR, HER2, HER3, and RET in lung cancer cells positive for MET amplification. ( A ) Serum-deprived EBC-1 and H1993 cells were incubated for 2 h in the absence or presence of PHA-665752 (500 n M ), lysed, and subjected to immunoprecipitation (IP) with antibodies to MET or control IgG. The resulting precipitates were subjected to immunoblot analysis with antibodies to the indicated proteins. ( B ) Serum-deprived cells were lysed and subjected to IP with antibodies to EGFR, to HER2, to HER3, or to RET, and the resulting precipitates were subjected to immunoblot analysis with antibodies to the indicated proteins.

Journal: British Journal of Cancer

Article Title: Differential roles of trans-phosphorylated EGFR, HER2, HER3, and RET as heterodimerisation partners of MET in lung cancer with MET amplification

doi: 10.1038/bjc.2011.322

Figure Lengend Snippet: Association of MET with EGFR, HER2, HER3, and RET in lung cancer cells positive for MET amplification. ( A ) Serum-deprived EBC-1 and H1993 cells were incubated for 2 h in the absence or presence of PHA-665752 (500 n M ), lysed, and subjected to immunoprecipitation (IP) with antibodies to MET or control IgG. The resulting precipitates were subjected to immunoblot analysis with antibodies to the indicated proteins. ( B ) Serum-deprived cells were lysed and subjected to IP with antibodies to EGFR, to HER2, to HER3, or to RET, and the resulting precipitates were subjected to immunoblot analysis with antibodies to the indicated proteins.

Article Snippet: Rabbit polyclonal antibodies to phosphorylated human MET (pY1234/pY1235), to phosphorylated EGFR (pY1068), to phosphorylated HER2 (pY1221), to phosphorylated HER3 (pY1289), to phosphorylated RET (pY905), to AKT, to phosphorylated AKT, to signal transducer and activator of transcription 3 (STAT3), to phosphorylated STAT3, and to poly(ADP-ribose) polymerase (PARP) were obtained from Cell Signaling Technology (Danvers, MA, USA); those to HER3, to RET, to extracellular signal-regulated kinase (ERK), and to phosphorylated ERK were from Santa Cruz Biotechnology (Santa Cruz, CA, USA); those to MET were from Zymed (South San Francisco, CA, USA); those to HER2 were from Millipore (Billerica, MA, USA); and those to β -actin were from Sigma.

Techniques: Amplification, Incubation, Immunoprecipitation, Control, Western Blot

Effects of depletion of MET, EGFR, HER2, HER3, or RET on cell proliferation, apoptosis, and migration in lung cancer cells with MET amplification ( A ), EBC-1 and H1993 cells were transfected with MET, EGFR, HER2, HER3, RET, or nonspecific (Con) siRNAs for 72 h, after which cell lysates were prepared and subjected to immunoblot analysis with antibodies to the indicated proteins. ( B ) Cells transfected as in ( A ) were evaluated for cell proliferation. Absorbance values were expressed as a percentage of that for cells transfected with a control siRNA. ( C ) Cells transfected as in ( A ) were evaluated for the proportion of apoptotic cells. Data are expressed as the percentage increase in the number of annexin V-positive cells relative to the corresponding value for cells transfected with a control siRNA. ( D ) Cells were transfected with the indicated siRNAs for 24 h and then transferred in serum-free medium to cell culture inserts of a transwell apparatus for 24 h. The number of cells that migrated toward complete medium was counted with the use of a light microscope. Data are expressed relative to the value for cells transfected with a control siRNA. Data in ( B – D ) are means±s.e. from three independent experiments.

Journal: British Journal of Cancer

Article Title: Differential roles of trans-phosphorylated EGFR, HER2, HER3, and RET as heterodimerisation partners of MET in lung cancer with MET amplification

doi: 10.1038/bjc.2011.322

Figure Lengend Snippet: Effects of depletion of MET, EGFR, HER2, HER3, or RET on cell proliferation, apoptosis, and migration in lung cancer cells with MET amplification ( A ), EBC-1 and H1993 cells were transfected with MET, EGFR, HER2, HER3, RET, or nonspecific (Con) siRNAs for 72 h, after which cell lysates were prepared and subjected to immunoblot analysis with antibodies to the indicated proteins. ( B ) Cells transfected as in ( A ) were evaluated for cell proliferation. Absorbance values were expressed as a percentage of that for cells transfected with a control siRNA. ( C ) Cells transfected as in ( A ) were evaluated for the proportion of apoptotic cells. Data are expressed as the percentage increase in the number of annexin V-positive cells relative to the corresponding value for cells transfected with a control siRNA. ( D ) Cells were transfected with the indicated siRNAs for 24 h and then transferred in serum-free medium to cell culture inserts of a transwell apparatus for 24 h. The number of cells that migrated toward complete medium was counted with the use of a light microscope. Data are expressed relative to the value for cells transfected with a control siRNA. Data in ( B – D ) are means±s.e. from three independent experiments.

Article Snippet: Rabbit polyclonal antibodies to phosphorylated human MET (pY1234/pY1235), to phosphorylated EGFR (pY1068), to phosphorylated HER2 (pY1221), to phosphorylated HER3 (pY1289), to phosphorylated RET (pY905), to AKT, to phosphorylated AKT, to signal transducer and activator of transcription 3 (STAT3), to phosphorylated STAT3, and to poly(ADP-ribose) polymerase (PARP) were obtained from Cell Signaling Technology (Danvers, MA, USA); those to HER3, to RET, to extracellular signal-regulated kinase (ERK), and to phosphorylated ERK were from Santa Cruz Biotechnology (Santa Cruz, CA, USA); those to MET were from Zymed (South San Francisco, CA, USA); those to HER2 were from Millipore (Billerica, MA, USA); and those to β -actin were from Sigma.

Techniques: Migration, Amplification, Transfection, Western Blot, Control, Cell Culture, Light Microscopy

Proposed model for the roles of signalling pathways activated by heterodimers of MET and either EGFR, HER2, HER3, or RET in lung cancer cells with MET amplification.

Journal: British Journal of Cancer

Article Title: Differential roles of trans-phosphorylated EGFR, HER2, HER3, and RET as heterodimerisation partners of MET in lung cancer with MET amplification

doi: 10.1038/bjc.2011.322

Figure Lengend Snippet: Proposed model for the roles of signalling pathways activated by heterodimers of MET and either EGFR, HER2, HER3, or RET in lung cancer cells with MET amplification.

Article Snippet: Rabbit polyclonal antibodies to phosphorylated human MET (pY1234/pY1235), to phosphorylated EGFR (pY1068), to phosphorylated HER2 (pY1221), to phosphorylated HER3 (pY1289), to phosphorylated RET (pY905), to AKT, to phosphorylated AKT, to signal transducer and activator of transcription 3 (STAT3), to phosphorylated STAT3, and to poly(ADP-ribose) polymerase (PARP) were obtained from Cell Signaling Technology (Danvers, MA, USA); those to HER3, to RET, to extracellular signal-regulated kinase (ERK), and to phosphorylated ERK were from Santa Cruz Biotechnology (Santa Cruz, CA, USA); those to MET were from Zymed (South San Francisco, CA, USA); those to HER2 were from Millipore (Billerica, MA, USA); and those to β -actin were from Sigma.

Techniques: Amplification