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Documenti fondamentali

SAB3700834

Sigma-Aldrich

Anti-Rabbit IgG F(ab′)2, highly cross adsorbed-Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

ALP, Alk Phos

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.46

Origine biologica

goat

Livello qualitativo

Coniugato

alkaline phosphatase conjugate

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

secondary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

Reattività contro le specie

rabbit

Concentrazione

0.69 mg/mL

tecniche

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

modifica post-traduzionali bersaglio

unmodified

Descrizione generale

Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as Fragment antigen binding (Fab) fragments. These fragments contain the light chains paired with the VH and CH1 domains of the heavy chains.
Immunoglobulin G (IgG) is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. It belongs to the immunoglobulin family and is a widely expressed serum antibody. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as Fragment antigen binding (Fab) fragments. These fragments contain the light chains paired with the VH and CH1 domains of the heavy chains.

Specificità

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Rabbit IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Alkaline Phosphatase (calf intestine), Anti-Goat Serum, Rabbit IgG, Rabbit IgG F(ab′)2 and Rabbit Serum. No reaction was observed against Rabbit IgG F(c) or Human Serum Proteins.

Immunogeno

Rabbit IgG F(ab′)2 fragment

Proprietà fisiche

Antibody format: IgG

Stato fisico

Supplied in 0.05 M Tris Chloride, 0.15M Sodium Chloride, 0.001M Magnesium Chloride, 0.0001M Zinc Chloride, 50% (v/v) Glycerol; pH 8.0 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)

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