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Key Documents

371732

Sigma-Aldrich

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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

100

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

isotype

IgG

shipped in

wet ice

storage temp.

−70°C

target post-translational modification

unmodified

Gene Information

human ... GNAI1(2770)

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

Application

Immunoblotting (1:1000)

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 (-70°C).

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)

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.

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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+
Valeria Burghi et al.
The Journal of biological chemistry, 299(11), 105293-105293 (2023-09-30)
β-arrestins play a key role in G protein-coupled receptor (GPCR) internalization, trafficking, and signaling. Whether β-arrestins act independently of G protein-mediated signaling has not been fully elucidated. Studies using genome-editing approaches revealed that whereas G proteins are essential for mitogen-activated
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