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G6666

Sigma-Aldrich

Monoclonal Anti-GAP1IP4BP antibody produced in mouse

~2 mg/mL, clone GP-3, purified immunoglobulin, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

GP-3, monoclonal

form

buffered aqueous solution

mol wt

antigen ~100 kDa

species reactivity

human

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using human platelets extract

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... RASA3(22821)

General description

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

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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P J Cullen et al.
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
J R Bottomley et al.
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
S S El-Daher et al.
Blood, 95(11), 3412-3422 (2000-05-29)
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
P J Cullen et al.
Nature, 376(6540), 527-530 (1995-08-10)
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
P J Lockyer et al.
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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