Phospho-Zyxin (Ser142/143) (D1

8467:

Immunoprecipitation , Western Blotting

Phospho-Zyxin (Ser142/143) (D1E8) Rabbit mAb recognizes endogenous levels of zyxin protein only when phosphorylated at Ser142 and Ser143.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser142 and Ser143 of human zyxin protein.

Western Blotting

Western blot analysis of extracts from A-431 and U-2 OS cells, untreated (-) or treated (+) with λ and calf intestinal phosphatase (λ/CIP), using Phospho-Zyxin (Ser142/143) (D1E8) Rabbit mAb (upper) or Zyxin Antibody #3553 (lower).

IP

Immunoprecipitation of extracts from A-431 cells using Phospho-Zyxin (Ser142/143) (D1E8) Rabbit mAb. Western blot was performed using the same antibody. Lane 1 is 10% input.

The Ras superfamily of small GTP-binding proteins (G proteins) comprise a large class of proteins (over 150 members) that can be classified into at least five families based on their sequence and functional similarities: Ras, Rho, Rab, Arf, and Ran (1-3). These small G proteins have both GDP/GTP-binding and GTPase activities and function as binary switches in diverse cellular and developmental events that include cell cycle progression, cell survival, actin cytoskeletal organization, cell polarity and movement, and vesicular and nuclear transport (1). An upstream signal stimulates the dissociation of GDP from the GDP-bound form (inactive), which leads to the binding of GTP and formation of the GTP-bound form (active). The activated G protein then goes through a conformational change in its downstream effector-binding region, leading to the binding and regulation of downstream effectors. This activation can be switched off by the intrinsic GTPase activity, which hydrolyzes GTP to GDP and releases the downstream effectors. These intrinsic guanine nucleotide exchange and GTP hydrolysis activities of Ras superfamily proteins are also regulated by guanine nucleotide exchange factors (GEFs) that promote formation of the active GTP-bound form and GTPase activating proteins (GAPs) that return the GTPase to its GDP-bound inactive form (4).

1. Takai, Y. et al. (2001) Physiol Rev 81, 153-208.
2. Colicelli, J. (2004) Sci STKE 2004, RE13.
3. Wennerberg, K. et al. (2005) J Cell Sci 118, 843-6.
4. Vigil, D. et al. (2010) Nat Rev Cancer 10, 842-57.

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For Research Use Only. Not For Use In Diagnostic Procedures.