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G7402

Sigma-Aldrich

Anti-Rabbit IgG (whole molecule)–Gold antibody produced in goat

affinity isolated antibody, aqueous glycerol suspension, 10 nm (colloidal gold)

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

goat

Conjugué

gold conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

aqueous glycerol suspension

Technique(s)

dot blot: suitable
western blot: suitable

Taille des particules

10 nm (colloidal gold)

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

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Catégories apparentées

Description générale

IgG antibody plays a crucial role in humoral immune responses such as complement activation, phagocytosis, placental transport and cell surface-receptor binding. Anti-rabbit IgG (whole molecule)-gold antibody can be used as secondary antibody (diluted 1:50 in 0.01 M PBS containing 1% BSA and 5% NGS) in EM immunolabeling of GABA and glutamate by postembedding procedure. It can also be used in a modified dot blot assay to determine binding activity. Goat anti-rabbit IgG (whole molecule)-gold antibody reacts specifically with all goat immunoglobulins.
Immunoglobulins (Igs) are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs can be useful tools for the analysis of target proteins
Anti-Rabbit IgG (whole molecule)-Gold antibody is specific for rabbit IgG.

Immunogène

Rabbit IgG purified from normal rabbit serum.

Application

Anti-rabbit IgG (whole molecule)-gold antibody (diluted 1: 15) can be used in immunoelectron microscopy. It can also be used in western blotting.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immuno-electron microscopy (1 paper)
Immunohistochemistry (1 paper)

Forme physique

Colloidal suspension in Tris buffered saline, pH 8.2, with 30% glycerol (v/v), 1% bovine serum albumin (w/v), and 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Vladimir Varga et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(32), E6546-E6555 (2017-07-21)
The distal end of the eukaryotic flagellum/cilium is important for axonemal growth and signaling and has distinct biomechanical properties. Specific flagellum tip structures exist, yet their composition, dynamics, and functions are largely unknown. We used biochemical approaches to identify seven
G Kamp et al.
Reproduction (Cambridge, England), 133(1), 29-40 (2007-01-25)
Glycolysis is crucial for sperm functions (motility and fertilization), but how this pathway is regulated in spermatozoa is not clear. This prompted to study the location and the regulatory properties of 6-phosphofructokinase (PFK, EC 2.7.1.11), the most important element for
Andrea González et al.
The American journal of tropical medicine and hygiene, 92(5), 887-897 (2015-03-12)
Trypanosoma cruzi calreticulin (TcCRT), a 47-kDa chaperone, translocates from the endoplasmic reticulum to the area of flagellum emergence. There, it binds to complement components C1 and mannan-binding lectin (MBL), thus acting as a main virulence factor, and inhibits the classical
S Sinnarajah et al.
FEBS letters, 426(3), 377-380 (1998-05-26)
The odorant-induced accumulation of cAMP can be inhibited by antibodies directed against G alpha s/olf. In contrast, antibodies raised against G alpha i-subunits caused a strong enhancement of the odorant-induced cAMP accumulation. Western blotting and immunoelectron microscopy revealed the presence
Ignaz Wessler et al.
PloS one, 11(6), e0156886-e0156886 (2016-06-11)
The worldwide use of neonicotinoid pesticides has caused concern on account of their involvement in the decline of bee populations, which are key pollinators in most ecosystems. Here we describe a role of non-neuronal acetylcholine (ACh) for breeding of Apis

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