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Merck

SAB3701027

Sigma-Aldrich

Anti-Mouse IgG (Fc specific), F(ab′)2 fragment, highly cross adsorbed antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.46

生物源

goat

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

secondary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

物種活性

mouse

濃度

1.0 mg/mL

技術

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

運輸包裝

wet ice

儲存溫度

2-8°C

目標翻譯後修改

unmodified

一般說明

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. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The Fc fragment contains the CH2 and CH3 domains of the antibody molecule. Pepsin cleaves the carboxy-terminal side of the disulfide bonds in the general region of the antibody and this gives rise to the F(ab′)2 fragment. The two antigen-binding arms of the antibody are linked in this fragment. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

特異性

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

免疫原

Mouse IgG F(c) fragment

物理性質

Antibody format: IgG F(ab′)2

外觀

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

免責聲明

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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儲存類別代碼

10 - Combustible liquids

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE
Journal of Reproductive Immunology (1997)
Janeway CA
Immunobiology (2001)
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences (2007)
Jian Zhang et al.
International journal of oncology, 45(2), 683-690 (2014-06-04)
Tanshinone IIA (TSIIA), a natural diterpene quinone in the traditional Chinese medicinal herb Dan-Shen (Salvia miltiorrhiza), has extensively exerted antitumor activity in cellular and animal models. However, the molecular mechanisms underlying the antitumor effects of TSIIA remain largely unknown. The
Debolina Ghosh et al.
Journal of Alzheimer's disease : JAD, 42(1), 313-324 (2014-05-23)
The extracellular redox environment of cells is mainly set by the redox couple cysteine/cystine (cys/cySS) while intracellular redox is buffered by reduced/oxidized glutathione (GSH/GSSG), but controlled by NAD(P)H/NAD(P). With aging, the extracellular redox environment shifts in the oxidized direction beyond

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