371729
Anti-Giα-3-Subunit, C-Terminal (345-354) Rabbit pAb
liquid, Calbiochem®
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
liquid
does not contain
preservative
species reactivity (predicted by homology)
mammals
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
unmodified
Gene Information
human ... GNAI3(2773)
General description
Anti-Giα-3-Subunit, C-Terminal (345-354), rabbit polyclonal, recognizes Giα-3 subunit. Does not cross-react with Gsα & Goα subunits. Validated for use in WB & IP.
Immunoaffinity purified rabbit polyclonal antibody. Recognizes the Giα-3 subunit protein.
Recognizes Giα-3 subunit. Does not cross-react with Gsα and Goα, but partially cross-reacts with Giα1-, G1α2-subunits.
Immunogen
a synthetic peptide (CKNNLKECGLY) corresponding to amino acids at the C-terminus of mammalian Giα-3, conjugated to KLH
Application
Immunoblotting (1:1000)
Immunoprecipitation (see comments)
Immunoprecipitation (see comments)
Warning
Toxicity: Standard Handling (A)
Physical form
In 140 mM NaCl, 100 mM potassium phosphate, pH 7.5.
Reconstitution
Following initial thaw, aliquot and freeze (-20°C).
Other Notes
Kumar, R., et al. 1994. J. Mol. Cell. Cardiol. 26, 1537.
Raymond, J.R., et al. 1993. Biochemistry32, 11064.
Mumby, S.M., and Gilman, A.G. 1991. Methods Enzymol.195, 215.
Jones, D.T., and Reed, R.R. 1987. J. Biol. Chem.262, 14,241.
Raymond, J.R., et al. 1993. Biochemistry32, 11064.
Mumby, S.M., and Gilman, A.G. 1991. Methods Enzymol.195, 215.
Jones, D.T., and Reed, R.R. 1987. J. Biol. Chem.262, 14,241.
The specificity was confirmed with lysates from separate cultures of bacteria transfected with the genes for Gsα, Giα-1, GIα-2, Giα-3, and Goα. The original titer of the serum was 1:10,000. Suitable for immunoblotting and immunoprecipitation. Does not cross-react with Gsα and Goα. Antibody partially cross-reacts with Giα-1 and GIα-2. Variables associated with assay conditions will dictate the proper working dilution.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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R R Mirotznik et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 20(20), 7614-7621 (2000-10-12)
The inhibition of presynaptic calcium channels via G-protein-dependent second messenger pathways is a key mechanism of transmitter release modulation. We used the calyx-type nerve terminal of the chick ciliary ganglion to examine which G-proteins are involved in the voltage-sensitive inhibition
C Chen et al.
The Journal of physiology, 491 ( Pt 1), 21-29 (1996-02-15)
1. Somatotroph-enriched cells (up to 85%) were obtained from ovine pituitary glands by means of collagenase dissociation and Percoll-gradient centrifugation. Further identification was based on the reduction in Ca2+ currents by 10 nM somatostatin (SRIF). 2. The whole-cell configuration of
Jun Cheng et al.
American journal of physiology. Heart and circulatory physiology, 302(7), H1454-H1465 (2012-01-31)
Calmodulin-dependent protein kinase II (CaMKII) has been proposed to be a therapeutic target for heart failure (HF). However, the cardiac effect of chronic CaMKII inhibition in HF has not been well understood. We have tested alterations of Ca(2+) handling, excitation-contraction
C Chen
The American journal of physiology, 275(2), E278-E284 (1998-08-04)
Voltage-gated K+ currents in rat somatotrophs are increased by somatostatin (SRIF) through unidentified G protein. In this experiment, somatotroph-enriched cells (up to 85%) were obtained from ovine pituitary glands and further identified by the increase in K+ currents by SRIF.
Heng Xu et al.
Brain research bulletin, 77(1), 49-54 (2008-07-22)
Recent evidence indicates that agonist ligands of G protein coupled receptors (GPCR) can activate different signaling systems. Such "agonist-directed" signaling also occurs with opioid receptors. Previous work from our laboratory showed that chronic morphine, but not DAMGO, up-regulates the expression
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