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Merck
CN

371732

Anti-Gsα-Subunit, C-Terminal (385-394) Rabbit pAb

liquid, Calbiochem®

别名:

Anti-Gₛα Antibody, Gₛα-Subunit Detection Antibody, Rabbit Anti-Gₛα-Subunit

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
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产品名称

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)

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.

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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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Susan E Sadler et al.
Developmental biology, 322(1), 199-207 (2008-08-19)
Treatment of Xenopus laevis oocytes with cholesterol-depleting methyl-beta-cyclodextrin (MebetaCD) stimulates phosphorylation of mitogen-activated protein kinase (MAPK) and oocyte maturation, as reported previously [Sadler, S.E., Jacobs, N.D., 2004. Stimulation of Xenopus laevis oocyte maturation by methyl-beta-cyclodextrin. Biol. Reprod. 70, 1685-1692.]. Here
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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