Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, R||IP, WB||Rb||Purified||Polyclonal Antibody|
|Application||Detect PIKE-L/S using this Anti-PIKE-L/S Antibody validated for use in IP & WB.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||stable for 2 years at -20°C from date of shipment|
|Material Size||200 µg|
|Anti-PIKE-L/S (rabbit polyclonal IgG) -2483898||2483898|
|Anti-PIKE-L/S - 30327||30327|
|Reference overview||Pub Med ID|
|PIKE GTPase: a novel mediator of phosphoinositide signaling.|
Ye, Keqiang and Snyder, Solomon H
J. Cell. Sci., 117: 155-61 (2004) 2004
Phosphoinositide (PI) 3-kinase enhancer (PIKE) is a brain-specific GTPase that binds to PI 3-kinase and stimulates its lipid kinase activity. It exists in two forms: the first to be identified, PIKE-S, is shorter and exclusively nuclear; by contrast, the longer form, PIKE-L, resides in multiple intracellular compartments. Nerve growth factor treatment leads to PIKE-S activation by triggering the nuclear translocation of phospholipase C (PLC)-gamma 1, which acts as a physiological guanine nucleotide exchange factor (GEF) for PIKE-S through its Src-homology 3 (SH3) domain. Cytoplasmic PI 3-kinase and its lipid product phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P3] regulate the membrane translocation and activation of many signaling molecules by binding to their pleckstrin homology (PH) domains. However, little is known about the physiological roles of their nuclear counterparts. The nuclear PLC-gamma 1/PIKE-S/PI 3-kinase signaling pathway seems to be an extension of the crosstalk between cytoplasmic PLC-gamma 1 and PI 3-kinase. PIKE-L contains a C-terminal extension consisting of an ADP ribosylation-GTPase-activating protein (ArfGAP) domain and two ankyrin repeats in addition to the N-terminal GTPase domain. PIKE-L could have additional, extranuclear functions, including regulation of postsynaptic signaling by metabotropic glutamate receptors.
|PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt.|
Ahn, Jee-Yin, et al.
Proc. Natl. Acad. Sci. U.S.A., 101: 6993-8 (2004) 2004
PIKE-A (PIKE-activating Akt), an isoform of PIKE GTPase that enhances phosphatidylinositol 3-kinase (PI3-kinase) activity, specifically binds to active Akt but not PI3-kinase. PIKE-A stimulates Akt activity in a GTP-dependent manner and promotes invasiveness of cancer cell lines. Here, we show that PIKE-A is amplified in a variety of human cancers and that amplified PIKE-A directly stimulates Akt and inhibits apoptosis compared to cells with normal PIKE-A copy number. Overexpression of PIKE-A wild-type but not dominant-negative mutant stimulates Akt activity and prevents apoptosis. Moreover, knockdown of PIKE-A diminishes Akt activity and increases apoptosis. Our findings suggest that PIKE-A amplification contributes to cancer cell survival and progression by inhibiting apoptosis through up-regulating Akt.
|Phospholipase C-gamma1: a phospholipase and guanine nucleotide exchange factor.|
Wang, Zhixiang and Moran, Michael F
Mol. Interv., 2: 352-5,338 (2002) 2002
Although phospholipase C-gamma (PLC-gamma) participates in cellular mitogenesis, evidence indicates that the catalytic activity of PLC-gamma (to hydrolyze certain phosphoinositides) is nonessential to the process. So how is it that PLC-gamma is necessary but its lipase activity is not? Recently published results from Snyder and colleagues describe the ability of PLC-gamma to facilitate guanine nucleotide exchange for the recently identified nucleus-localized GTPase PIKE, which acts to enhance the enzymatic activity of phosphatidylinositol 3'-kinase (PI3K). The authors contend that the SH3 domain, rather than the catalytic domain, of PLC-gamma is required for aiding PIKE, and furthermore, that the mitogenic activity of PLC-gamma depends not on its phospholipase activity, but rather on its interaction with PIKE. Wang and Moran examine the results and piece together a picture of how PLC-gamma cooperates with PIKE.