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G6541

Sigma-Aldrich

Monoclonal Anti-GRP1 antibody produced in mouse

~2 mg/mL, clone CYT3-10, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-ARNO3, Anti-Cytohesin-3

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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

CYT3-10, monoclonal

form

buffered aqueous solution

mol wt

antigen 45 kDa

species reactivity

rat, human

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 2-4 μg/mL using whole extract of cultured human NRK (normal rat kidney) cells

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CYTH3(9265)
rat ... Cyth3(116693)

Immunogen

recombinant human GRP1 (general receptor for phosphoinositides-1).

Application

Monoclonal Anti-GRP1 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 2-4μg/mL using whole extract of cultured human NRK (normal rat kidney) cells.

Biochem/physiol Actions

GRP1 gene encodes a protein belonging to the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. The members of this family contain an N-terminal coiled-coil motif that is involved in homodimerization, a central Sec7 domain with guanine-nucleotide exchange protein (GEP) activity, and a C-terminal pleckstrin homology (PH) domain that interacts with phospholipids and facilitates association of PSCDs with membranes. This protein is responsible for the control of Golgi structure and function via the activation of ARF1 on Golgi membrane. It is also involved in the regulation of ARF6 functions.

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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J K Klarlund et al.
The Journal of biological chemistry, 275(42), 32816-32821 (2000-07-27)
GRP1 and the related proteins ARNO and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. Here we show the PH domains of all three proteins
M Franco et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(17), 9926-9931 (1998-08-26)
Budding of transport vesicles in the Golgi apparatus requires the recruitment of coat proteins and is regulated by ADP ribosylation factor (ARF) 1. ARF1 activation is promoted by guanine nucleotide exchange factors (GEFs), which catalyze the transition to GTP-bound ARF1.
S E Langille et al.
The Journal of biological chemistry, 274(38), 27099-27104 (1999-09-10)
The GRP1 protein contains a Sec7 homology domain that catalyzes guanine nucleotide exchange on ADP-ribosylation factors (ARF) 1 and 5 as well as a pleckstrin homology domain that binds phosphatidylinositol(3,4,5)P(3), an intermediate in cell signaling by insulin and other extracellular
G Pacheco-Rodriguez et al.
The Journal of biological chemistry, 273(41), 26543-26548 (1998-10-03)
ADP-ribosylation factors (ARFs) are 20-kDa guanine nucleotide-binding proteins that require specific guanine nucleotide-exchange proteins (GEPs) to accelerate the conversion of inactive ARF-GDP to active ARF-GTP. Cytohesin-1, a 46-kDa ARF GEP, contains a central Sec7 domain of 188 amino acids similar
G E Cozier et al.
The Journal of biological chemistry, 275(36), 28261-28268 (2000-06-28)
The group I family of pleckstrin homology (PH) domains are characterized by their inherent ability to specifically bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) and its corresponding inositol head-group inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P(4)). In vivo this interaction results in the regulated plasma membrane recruitment

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