Buy ISO/IEC INFORMATION TECHNOLOGY – SECURITY TECHNIQUES – PRIVACY CAPABILITY ASSESSMENT MODEL from. received in the West for the same period, for example, /10 at com from 27, reviews; /10 at from 29, reviews). B_ Organism . ORF Names:B_Imported . a>Chaini PRO_, 1 – , Potassium channel B_Add BLAST,
|Published (Last):||20 August 2009|
|PDF File Size:||8.63 Mb|
|ePub File Size:||10.43 Mb|
|Price:||Free* [*Free Regsitration Required]|
Postage cost can’t be calculated. For double transfection experiments, T cells gift of Dr. Fast and safe postage.
Thus, co-expression of caveolin with c-Src can abolish its capacity for auto-phosphorylation, as predicted based on our experiments with caveolin peptides see Fig.
Terms and conditions apply. Representative APR variable Email to friends Share on Facebook – opens in a new window or tab Share on Twitter – opens in a new window or tab Share 291990 Pinterest – opens in a new window or tab Add to Watch list. Cells were then permeabilized with 0. Caveolin 92190 recombinantly expressed as a glutathione S -transferase fusion. For example, Shoelson and colleagues have shown that high concentrations of peptide substrates inhibited the autophosphorylation of c-Src kinase See all carpartsinmotion has no other items for xs.
To test this hypothesis, we assessed the interaction of caveolin with Src family tyrosine kinases in vitro using i baculovirus-expressed Src proteins c-Src and v-Src and ii bacterially expressed caveolin fusion proteins.
Brake Pads Set GDB TRW 2E Genuine Top Quality Replacement New | eBay
Kunxin Luo, Whitehead Institute, and Dr. Note that peptide 1 had no effect, whereas peptide 2 dose-dependently suppressed the auto-activation of Fyn. Co-expression with Caveolin Suppresses the Auto-activation 92190 c-Src in Vivo The experiments described above indicate that caveolin residues interact directly with c-Src and functionally suppress auto-activation of c-Src in vitro.
The SH2 domain recognizes specific phosphotyrosine based motifs 61whereas the SH3 domain binds proline-rich peptide sequences with the consensus P XX P 6263 For example, the expression of caveolin-3 is absolutely muscle-specific skeletal and cardiac muscle cells 20 Although immunoblot analysis indicates that these immunoprecipitates contain equivalent amounts of c-Src kinase, little or no kinase activity was associated with c-Src 2910 co-expressed with caveolin in vivo.
Portions of the information contained in this table have been provided by carpartsinmotion. Learn more – opens in new window or tab. 92190 of caveolin peptides on the auto-phosphoryation of c-Src and Fyn tyrosine kinases. Watch list is full. Pardee Foundation to M.
DS 428 DARK BROWN SMOOTH MATTE
Effects of caveolin peptides on the auto-activation of c-Src tyrosine kinase. This is consistent with results demonstrating co-immunoprecipitation of caveolin with c-Src using antibodies directed against c-Src Fig. In contrast, recombinant overexpression of wild-type c-Src does not result in efficient cell transformation or increased tyrosine phosphorylation, indicating that the tyrosine kinase activity of c-Src is normally repressed 37 Co-expression of c-Src and Caveolin in Mammalian T Cells Untagged caveolin and c-Src were co-expressed in T cells by co-transfection using a modified calcium phosphate precipitation procedure as described previously However, similar fusion containing caveolin residues did not show any interaction.
After preclearing, supernatants were transferred to tubes containing mouse monoclonal anti-Src IgG prebound to protein A-Sepharose. The functional existence of such a negative regulator or suppressor of c-Src has been suggested by earlier studies It should be noted that this band was not detectable in uninfected cells or in cells infected with vector alone not shown.
Select a valid country. The eluate was mixed 1: Anti-Src-immunoprecipitates from T cells co-transfected with c-Src and caveolin were washed twice with kinase reaction buffer 20 m M Hepes, pH 7. These cells express extremely low levels of endogenous caveolin; little or no immunoreactivity was observed with anti-caveolin IgG by Western blotting not shown.
Submit your work to JBC. Because mutations in the extreme C terminus, the kinase domain, the SH2 domain, or the SH3 domain can constitutively activate c-Src, this activation may be mediated a conformational change in one of these regions Search for related content.
Report item – opens in a new window or tab. As a consequence of C-terminal divergence, v-Src does not contain Tyrwhich when phosphorylated can act to functionally inactivate c-Src kinase Using purified recombinant c-Src tyrosine kinase, we evaluated the effects of these caveolin peptides on the functional auto-activation of c-Src kinase in vitro.
See the cs listing for full details.
Compatibility information isn’t available for this item.