DS 29190 PDF

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Such a conformational change could also be induced normally by unknown allosteric effectors.

Issues regarding compatibility should be resolved before purchasing. Thus, a given mammalian cell, such as smooth muscle cells or fibroblasts, may co-express up to three or four immunologically distinct caveolin protein products.

As we find with caveolin, each of these enzymes is inhibited when bound to AKAP 29 Quantitation was performed as detailed previously This listing is for the part or sub-assembly number shown below only.

Caveolin peptides contain caveolin residues,orrespectively Table I. The following four peptides were utilized: In direct support of these findings, caveolin was first identified as a major transformation-dependent v-Src substrate in Rous sarcoma virus-transformed cells Tyrosine is not phosphorylated when c-Src is inactive and is phosphorylated when c-Src is active 38 Acta Reviews in Cancerin press.

Articles by Lisanti, M. Caveolin, a kDa integral membrane protein 78is a major structural and regulatory component of caveolae membranes 7910 Peptides were synthesized using standard methodology and subjected to amino acid analysis and mass spectroscopy Massachusetts Intitute of Technology Biopolymers Laboratory to confirm their composition.

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DS 428 DARK BROWN SMOOTH MATTE

Quantitation of these experiments is provided in D. Co-expression with caveolin dramatically suppressed the tyrosine kinase activity of c-Src as measured via an immune complex kinase assay. How does caveolin binding negatively regulate c-Src auto-activation?

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In this window In a new window. Peptides derived from all three caveolins contain two conserved tyrosine residues marked by arrows in Fig.

These results imply that the interaction of caveolin with Src family kinases may serve to negatively regulate their functional activity. Learn More – opens in a new window or tab. Email to friends Share on Facebook – opens in a new window or tab Share on Twitter – opens in a new window or tab Share on Fs – opens in a new window or tab Add to Watch list.

These scaffolding proteins, Ste5p 7374AKAP 29307576and 77787980 may simultaneously associate with distinct classes of signaling proteins to form a signaling pathway or module. Horseradish peroxidase-conjugated secondary antibodies 1: All other reagents were as detailed previously 27 Phosphorylated proteins were visualized by autoradiography using an intensifying screen.

Immunofluorescence All reactions were performed at room temperature.

Go to My Garage. Recently, two caveolin-related proteins caveolin-2 and caveolin-3 have been identified and cloned; caveolin has been retermed caveolin The cell pellets were analyzed by both in vitro kinase assay and immunoblotting using anti-Src antibody. Localization of c-Src and caveolin within a single cell. The SH2 domain recognizes specific phosphotyrosine based motifs 61whereas the SH3 domain binds proline-rich peptide sequences with the consensus P XX P 6263 Seller’s payment instructions If you are unsure about any details in the listing please contact us, we are here to help.

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Effect of caveolin peptides on the auto-phosphoryation of c-Src and Fyn tyrosine kinases.

Pdyn (prodynorphin) | Gene Report | BioGPS

Be the first to write a review. First, it is required to form multivalent homo-oligomers of caveolin. These results with v-Src further demonstrate the specificity of the interaction between c-Src and caveolin. A caveolin peptide derived from this region residues functionally suppressed the auto-activation of purified recombinant c-Src tyrosine kinase and Fyn, a related Src family tyrosine kinase.

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Kunxin Luo, Whitehead Institute, and Dr. 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. Note that both c-Src and v-Src migrate at 60 kDa as indicated.

However, the tightly regulated tyrosine kinase activity of c-Src can be activated transiently by a number of growth factors 38 This amount is subject to change until you make payment.