Cell Signaling Technology

Product Pathways - Adhesion

Phospho-GIT2 (Tyr392) (D8N9A) Rabbit mAb #11873

Applications Reactivity Sensitivity MW (kDa) Isotype
W H (M) (R) Endogenous 85 Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-GIT2 (Tyr392) (D8N9A) Rabbit mAb recognizes endogenous levels of GIT2 protein only when phosphorylated at Tyr392. This antibody may cross-react weakly with other tyrosine-phosphorylated proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr392 of human GIT2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from U-2 OS cells, untreated (-) or CIP and λ phosphatase-treated (+), using Phospho-GIT2 (Tyr392) (D8N9A) Rabbit mAb (upper) or GIT2 (D11B8) Rabbit mAb #8072 (lower).

Background

G protein-coupled receptor (GPCR) kinase interacting proteins 1 and 2 (GIT1 and GIT2) are highly conserved, ubiquitous scaffold proteins involved in localized signaling to help regulate focal contact assembly and cytoskeletal dynamics. GIT proteins contain multiple interaction domains that allow interaction with small GTPases (including ARF, Rac, and cdc42), kinases (such as PAK and MEK), the Rho family GEF Pix, and the focal adhesion protein paxillin (reviewed in 1). GIT1 and GIT2 share many of the same properties, but with at least ten distinct, tissue-specific splice variants. GIT2 has been shown to play an important role in inhibiting focal adhesion turnover and membrane protrusion (2,3). Focal adhesion localization and paxillin binding of GIT2 is regulated through phosphorylation at one or more tyrosine sites (Tyr286, Tyr392, Tyr592) by FAK and/or Src (4,5,reviewed in 6). Once at the focal adhesion, GIT2 is thought to play a key role in cell polarity and migration, making it a protein of interest in the investigation of oncogenic signaling pathways (3,5,7).

  1. Hoefen, R.J. and Berk, B.C. (2006) J Cell Sci 119, 1469-75.
  2. Premont, R.T. et al. (2000) J Biol Chem 275, 22373-80.
  3. Frank, S.R. et al. (2006) EMBO J 25, 1848-59.
  4. Brown, M.C. et al. (2005) Mol Biol Cell 16, 4316-28.
  5. Yu, J.A. et al. (2009) Mol Biol Cell 20, 4706-19.
  6. Yu, J.A. et al. Cell Adh Migr 4, 342-7.
  7. Mazaki, Y. et al. (2006) Nat Immunol 7, 724-31.

Application References

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Companion Products

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

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