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Key Documents

371732

Sigma-Aldrich

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

liquid, Calbiochem®

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

liquid

Ne contient pas

preservative

Réactivité de l'espèce (prédite par homologie)

mammals

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
avoid repeated freeze/thaw cycles

Isotype

IgG

Conditions d'expédition

wet ice

Température de stockage

−70°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... GNAI1(2770)

Description générale

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.

Immunogène

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)

Avertissement

Toxicity: Standard Handling (A)

Forme physique

In 140 mM NaCl, 100 mM potassium phosphate, pH 7.5.

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Remarque sur l'analyse

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)

Autres remarques

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.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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, 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
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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