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Principaux documents

371729

Sigma-Aldrich

Anti-Giα-3-Subunit, C-Terminal (345-354) Rabbit pAb

liquid, Calbiochem®

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.43

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated 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 ... GNAI3(2773)

Description générale

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.

Immunogène

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)

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 (-20°C).

Autres remarques

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.
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.

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

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
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
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
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.
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

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