G6541
Monoclonal Anti-GRP1 antibody produced in mouse
~2 mg/mL, clone CYT3-10, purified immunoglobulin, buffered aqueous solution
别名:
Anti-ARNO3, Anti-Cytohesin-3
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UNSPSC Code:
12352203
MDL number:
Conjugate:
unconjugated
Clone:
CYT3-10, monoclonal
Application:
ARR, ELISA (i), ICC, WB
Citations:
5
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
Quality Level
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
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
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.
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
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
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