G4290
Anti-Gαq11, C-Terminal antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human, mouse
technique(s)
immunoprecipitation (IP): suitable
western blot: 1:500-1:2,000 using rat brain microsomal preparation (20 μg)
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GNAQ(2776)
mouse ... Gnaq(14682)
General description
G-proteins are membrane associated heterotrimeric proteins comprising of α-, β-, and γ-subunits. The α-subunit contains a guanine-binding domain that is in an inactive state when it is occupied by GDP. Upon activation, GDP is replaced with GTP, causing the dissociation of the α-subunit from the βγ-subunit complex. This enables the Gα-GTP complex to bind to and regulate specific signaling pathways. GTP is then hydrolyzed, allowing for re-association of the α-subunit with the βγ-subunit complex.
Specificity
The sequence is highly conserved among species. The antibody is specific for Gαq11 and Gαq.
Immunogen
synthetic peptide corresponding to amino acids 350-359 of Gαq11 or amino acids 344-353 of Gαq.
Application
Anti-Gαq11, C-terminal antibody produced in rabbit is suitable for immunoprecipitation and western blot analysis at a working dilution of 1:500-1:2000 using 20μg of rat brain microsomal preparation.
Biochem/physiol Actions
Gq α (G11α) regulates the action of phospholipase C (PLC), and results in the release of other intracellular messengers through the inositol phosphate pathway, leading to the release of Ca2+ and the activation of phosphorylation.
Physical form
Solution in phosphate buffered saline, pH 7.4.
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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Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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B Kühn et al.
Molecular endocrinology (Baltimore, Md.), 10(12), 1697-1707 (1996-12-01)
In several cell systems histamine has been shown to stimulate both adenylyl cyclase and phospholipase C through activation of a G protein-coupled H2 receptor. To analyze the bifurcating signal emanating from the activated H2 receptor and to identify the G
M C Gong et al.
Molecular biology of the cell, 8(2), 279-286 (1997-02-01)
Prolonged treatment with guanosine 5'-[gamma-thio]triphosphate (GTP gamma S; 5-16 h, 50 microM) of smooth muscle permeabilized with Staphylococcus aureus alpha-toxin down-regulated (abolished) the acute Ca2+ sensitization of force by GTP gamma S, AIF-4, phenylephrine, and endothelin, but not the response
M Côté et al.
Endocrinology, 138(8), 3299-3307 (1997-08-01)
In 3-day primary cultures of rat glomerulosa cells, a 30-min pre-incubation with either 10 microM colchicine (a microtubule-disrupting agent) or 10 microM cytochalasin B (a microfilament-disrupting agent) decreased angiotensin II (Ang II)-induced inositol phosphate accumulation by 50%. Moreover, both drugs
Alpay Burak Seven et al.
Cell reports, 30(11), 3699-3709 (2020-03-04)
Many chaperones promote nascent polypeptide folding followed by substrate release through ATP-dependent conformational changes. Here we show cryoEM structures of Gα subunit folding intermediates in complex with full-length Ric-8A, a unique chaperone-client system in which substrate release is facilitated by
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