Phospho-GIT2 (Tyr392) (D8N9A) Rabbit mAb #11873
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 85 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
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.
Species Reactivity:
Human
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr392 of human GIT2 protein.
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 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).
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