anchored protein

Lipid anchored proteins are found within the lipid bilayer.

Cytoskeletally anchored proteins are differentially marked.

Cytoskeletal anchored proteins were precipitated with anti α V and β 6 -antibodies.

Cytoskeletal anchored proteins were extracted, co-immunoprecipitated (IP) and analyzed (Blot) with the antibodies indicated.

Lipid anchored proteins are covalently attached to different fatty acid acyl chains on the cytoplasmic side of the cell membrane via palmitoylation, myristoylation, or prenylation.

At the cell surface, on the opposite side of the cell membrane lipid anchored proteins are covalently attached to the lipids glycosylphosphatidylinositol (GPI) and cholesterol.

Thus the RBCs are not protected by GPI anchored proteins such as DAF.

To further support this finding, we stimulated cells and performed co-immunoprecipitated various integrin subunits of cytoskeletal anchored proteins [ 66 67 ] (additional file 1, 2, 3and 4).

Notably, tyrosine phosphorylation of cytoskeletally anchored proteins is further enhanced after combined treatment with mature TGFβ 1 and fibronectin in TGFβ 1 sensitive cells (Figure 3).

Cytoskeletal anchored proteins were extracted, and analyzed (Blot) with secondary antibodies (α-mouse HRP plus α-rabbit HRP plus α-goat HRP conjugated antibodies.)

The axon hillock also functions as a tight junction, since it acts as a barrier for lateral diffusion of transmembrane proteins, GPI anchored proteins such as thy1, and lipids embedded in the plasma membrane.

Thy-1, like many other GPI anchored proteins can be shed by special types of Phospholipase C e.g. PI-PLC (phosphatidyl-Inositol Phospholipase C, or PLC β).