371732
Anti-Gsα-Subunit, C-Terminal (385-394) Rabbit pAb
liquid, Calbiochem®
Synonym(s):
Anti-Gₛα Antibody, Gₛα-Subunit Detection Antibody, Rabbit Anti-Gₛα-Subunit
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Anti-Gsα-Subunit, C-Terminal (385-394) Rabbit pAb, liquid, Calbiochem®
biological source
rabbit
antibody form
purified 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
dilution
(Immunoblotting (1:1000))
isotype
IgG
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... GNAI1(2770)
Analysis Note
Positive Control
Gsα-Subunit, His•Tag, Rat Brain, Recombinant, E. coli (Cat. No. 371765) or Gsα-Subunit, Recombinant, E. coli, Immunoblot Standard (Cat. No. 371764)
Gsα-Subunit, His•Tag, Rat Brain, Recombinant, E. coli (Cat. No. 371765) or Gsα-Subunit, Recombinant, E. coli, Immunoblot Standard (Cat. No. 371764)
Application
Immunoblotting (1:1000)
Disclaimer
Toxicity: Standard Handling (A)
General description
Anti-Gsα-Subunit, C-Terminal (385-394), rabbit polyclonal, recognizes both large and small forms of Gsα-subunit. It is validated for use in Western blotting.
Protein A purified rabbit polyclonal antibody. Recognizes the ~40-45 kDa Gsα subunit protein.
Recognizes both large and small forms of Gsα-subunit. Does not cross-react with Giα-1-, Giα-2-, Giα-3-, or Goα-subunits.
Immunogen
a synthetic peptide (RMHLRQYELL) (Cat. No. 371782) corresponding to amino acids at the C-terminus of mammalian Gsα subunit, conjugated to KLH
Other Notes
Does not cross-react with Giα-1, Giα-2, Giα-3, or Goα. The specificity and cross-reactivity were confirmed with lysates from separate cultures of bacteria transfected with the genes for Gsα, Giα-1, GIα-2, Giα-3, and Goα. Variables associated with assay conditions will dictate the proper working dilution.
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.
Raymond, J.R., et al. 1993. Biochemistry32, 11064.
Mumby, S.M., and Gilman, A.G. 1991. Methods Enzymol.195, 215.
Physical form
In 140 mM NaCl, 100 mM potassium phosphate, pH 7.5.
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
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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P Viard et al.
British journal of pharmacology, 129(7), 1497-1505 (2000-04-01)
1. The effects of beta(3)-adrenergic stimulation were studied on the L-type Ca(2+) channel in single myocytes from rat portal vein using the whole-cell mode of the patch-clamp technique. 2. Reverse transcription-polymerase chain reaction showed that beta(1)-, beta(2)- and beta(3)-adrenoceptor subtypes
Shigeki Kamitani et al.
The FEBS journal, 278(15), 2702-2712 (2011-06-01)
Pasteurella multocida toxin (PMT) is a virulence factor responsible for the pathogenesis of some Pasteurellosis. PMT exerts its toxic effects through the activation of heterotrimeric GTPase (G(q), G(12/13) and G(i))-dependent pathways, by deamidating a glutamine residue in the α subunit
Enhanced sensitivity to cholera toxin in female ADP-ribosylarginine hydrolase (ARH1)-deficient mice.
Kizuku Watanabe et al.
PloS one, 13(11), e0207693-e0207693 (2018-12-01)
Cholera toxin, an 84-kDa multimeric protein and a major virulence factor of Vibrio cholerae, uses the ADP-ribosyltransferase activity of its A subunit to intoxicate host cells. ADP-ribosylation is a posttranslational modification of proteins, in which the ADP-ribose moiety of NAD+
An inducible explant model of osteoclast-osteoprogenitor coordination in exacerbated osteoclastogenesis.
Whitlock, et al.
iScience, 26, 106470-106470 (2023)
P Viard et al.
British journal of pharmacology, 132(3), 669-676 (2001-02-13)
1. Previous data have shown that activation of beta(3)-adrenoceptors stimulates vascular L-type Ca(2+) channels through a G alphas-induced stimulation of the cyclic AMP/PKA pathway. The present study investigated whether beta-adrenergic stimulation also uses the G beta gamma/PI3K/PKC pathway to modulate
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