Pathway Explorer Antibody MiniPack:
Each Pathway Explorer Antibody Minipack contains three related antibodies as part of a signaling cascade or a combination of total and phosphorylated forms of key signaling targets. Each of the three antibodies are 30% the original pack size. Full size versions of each of the Pathway Explorer antibodies are available for sale individually under the same catalog number with the removal of “SP” off of each one (e.g. 05-591SP can be ordered as 05-591).
Src:
Src is a family of proto-oncogenic tyrosine kinases originally discovered by J. Michael Bishop and Harold E. Varmus. Some tumor-inducing retroviruses (such as Rous sarcoma virus (RSV)), contain a gene called v-src (viral-sarcoma). It was found that the v-src gene in RSV is required for the formation of cancer. Hallmarks of v-src induced transformation are rounding of the cell and the formation of actin rich podosomes on the basal surface of the cell. These structures are correlated with increased invasiveness, a process thought to be essential for metastasis. V-src lacks the C-terminal inhibitory phosphorylation site, and is therefore constitutively active as opposed to normal src (c-src) which is only activated under certain circumstances where it is required (e.g. growth factor signaling). V-src is therefore an instructive example of an oncogene whereas c-src is a proto-oncogene.
FAK:
Focal adhesion kinase (FAK) is a cytoplasmic protein tyrosine kinase that has been implicated to play an important role in integrin-mediated signal transduction pathways. FAK becomes activated and tyrosine phosphorylated in integrin-mediated cell adhesion and is co-localized with integrins and other cytoskeletal proteins in focal contacts in a variety of adherent cells. Physical interactions of FAK with the integrin cytoplasmic domain as well as cytoskeletal proteins talin, paxillin, and/ or tensin have been proposed to play a key role in FAK activation by facilitating its oligomerization and transphosphorylation. FAK shows a rapid increase in tyrosine phosphorylation when stimulated by diverse signaling molecules, including those that regulate embryonic development, cell proliferation, migration and apoptosis, and efficient study methods are in high demand.
Paxillin:
Paxillin, a focal adhesion scaffolding protein, is phosphorylated on multiple tyrosine residues in response various stimulations including integrin stimulation, growth factor stimulation, and oncogenic transformation (v-Src, v-Crk and BCR/ABL). Paxillin binds many other focal adhesion proteins including FAK, Vinculin, Talin, and Tensin. As such, Paxillin and it tyrosine phosphorylation, help regulate the dynamics of the focal adhesions and the actin cytoskeleton which results in cell morphology and cell migration characteristics of the cell. Paxillin is most notable phosphorylated on tyrosines 31 and 118 (Tyr31 and Tyr118). Interestingly, Vinculin and FAK bind to overlapping sites on Paxillin. Additionally, there is an increase in Paxillin phosphorylation at Tyr118 in vinculin (-/-) and Vinculin Y822F cells. Paxillin Y31F Y118F expression restores apoptosis and inhibits Erk activity.
*See full size versions for corresponding references.