GAP1IP4BP is an IP4 receptor and belongs to the GAP1 family of GTPases activating proteins for the Ras family of GTPases (GAPs). It has N-terminal coupled C2 domains, highly conserved central Ras GAP domains and a C-terminal IP4-binding pleckstrin homology (PH) domain. This PH domain is linked to a 26-amino acid Btk (Bruton′s tyrosine kinase) motif (PH/Btk). GAP1IP4BP is widely expressed in tissues and is localized to the plasma membrane.
Immunogen
recombinant human GAP1IP4BP
Application
Monoclonal Anti-GAP1IP4BP antibody produced in mouse is suitable for immunocytochemistry, indirect ELISA and microarray. It is also suitable for western blot analysis at a working concentration of 1-2μg/mL using human platelets extract.
Biochem/physiol Actions
The binding activity of GAP1IP4BP depends on a functional PH/Btk domain. This domain binds to IP4 and targets the protein to the plasma membrane. This may facilitate the regulation of GAP1IP4BP by IP4. GAP1IP4BP is involved in the cation influx that is localized to the plasma membrane of human platelets.It plays a key role in Ca2+ regulation.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
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The Biochemical journal, 305 ( Pt 1), 139-143 (1995-01-01)
A novel Ins(1,3,4,5)P4-binding protein has been purified to apparent homogeneity from solubilized membranes derived from pig platelets. It has a high affinity for Ins(1,3,4,5)P4 (Kd 6.3 +/- 0.4 nM), a Bmax of 2.5-6.0 nmol/mg of protein, and a high specificity
Biochemical and biophysical research communications, 250(1), 143-149 (1998-09-15)
Previously we have purified and cloned a high affinity isomerically specific inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4)-binding protein which, because it is clearly a member of the GAP1 family of Ras GTPase-activating proteins (GAP), we have termed GAP1(IP4BP). Here we show that expressed
Platelet activation is associated with an increase of cytosolic Ca(++) levels. The (1,4,5)IP(3) receptors [(1,4,5)IP(3)R] are known to mediate Ca(++) release from intracellular stores of many cell types. Currently there are at least 3 distinct subtypes of (1,4, 5)IP(3)R-type I
Inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) is produced rapidly from inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) in stimulated cells. Despite extensive experimentation, no clearly defined cellular function has yet been described for this inositol phosphate. Binding sites specific for Ins(1,3,4,5)P4 have been identified in several tissues
Biochemical and biophysical research communications, 255(2), 421-426 (1999-03-02)
GAP1(IP4BP) and GAP1(m) belong to the GAP1 family of Ras GTPase-activating proteins that are candidate InsP4 receptors. Here we show they are ubiquitously expressed in human tissues and are likely to have tissue-specific splice variants. Analysis by subcellular fractionation of
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