Phospho-DAPP1/BAM32 (Tyr139) (D7G4G) Rabbit mAb #13703
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 29 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
| Immunoprecipitation | 1:200 |
Storage
Protocol
Specificity / Sensitivity
Phospho-DAPP1/BAM32 (Tyr139) (D7G4G) Rabbit mAb recognizes endogenous levels of DAPP1/BAM32 protein only when phosphorylated at Tyr139.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr139 of human DAPP1/BAM32 protein.
Background
The dual adaptor of phosphotyrosine and 3-phosphoinositides (DAPP1/BAM32) is a cytoplasmic adaptor protein that mediates the recruitment and interaction of molecules required for signal transduction downstream of the B cell receptor (BCR) (1). The DAPP1/BAM32 protein contains an amino-terminal SH2 domain and a carboxy-terminal pleckstrin homology (PH) domain that binds to PI3K-derived phosphoinositides (i.e., PIP3). Upon BCR activation, DAPP1/BAM32 is phosphorylated at specific tyrosine residues and translocated from the cytoplasm to the membrane. Research studies indicate that phosphorylation and translocation of DAPP1/BAM32 is strongly dependent upon PI3K signaling (2,3). The amino-terminal SH2 domain binds to PLCγ2 and other tyrosine-phosphorylated targets. As a result of these interactions, DAPP1/BAM32 can adjust the response to receptor activation by coordinating membrane-localized interactions among proteins of distinct signal transduction pathways (1,4). DAPP1/BAM32 is expressed most abundantly in B lymphocytes; high expression during dendritic cell (DC) maturation and localization to contact sites between DC and allogenic T cells suggest that the DAPP1/BAM32 adaptor may play a role in the activation of T cells through MHC class I-mediated signaling pathways (5).
Research studies show that phosphorylation of DAPP1/BAM32 at Tyr139 is PI3K-dependent, requires an intact PH domain in DAPP1/BAM32, and is likely performed by Src-family kinases following membrane recruitment of DAPP1/BAM32 by phosphoinositides (6). Blocking phosphorylation of DAPP1/BAM32 at Tyr139 inhibits BCR internalization and reduces cellular F-actin levels, suggesting that phosphorylation of DAPP1/BAM32 may play a role in regulating actin-dependent internalization of the activated BCR (7,8).
- Marshall, A.J. et al. (2007) Biochem Soc Trans 35, 181-2.
- Marshall, A.J. et al. (2000) J Exp Med 191, 1319-32.
- Anderson, K.E. et al. (2000) Curr Biol 10, 1403-12.
- Richards, S. et al. (2008) Immunol Rev 224, 183-200.
- Ortner, D. et al. (2011) J Immunol 187, 3972-8.
- Dowler, S. et al. (2000) Biochem J 349, 605-10.
- Niiro, H. et al. (2004) J Immunol 173, 5601-9.
- Allam, A. et al. (2004) J Biol Chem 279, 39775-82.
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