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B1395

Sigma-Aldrich

Anti-Bovine IgG (whole molecule) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.46

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

secondary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

tecniche

indirect ELISA: 1:150,000
quantitative precipitin assay: 2.0 mg/mL

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

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Descrizione generale

Immunoglobulins (Igs) belong to the immunoglobulin super-family. Each immunoglobin has two heavy (H) and two light (L) chains, held together by disulphide linkages. Heavy chain has one variable N-terminal region and three or four constant (CH1-CH4) C-terminal region. Each light chain comprises of one variable N-terminal region and a constant C-terminal region. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4, among them IgG1 is most abundant.

Applicazioni

Anti-Bovine IgG (whole molecule) antibody produced in rabbit may be used for indirect ELISA at a working dilution of 1:150,000. It was used in fluorescence immunoassay for quantitative determination of IgG in bovine milk.

Azioni biochim/fisiol

Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection. IgG antibody have enormous therapeutic potential and the Fc region is involved in the development of therapeutic antibody.
Digestion of IgG by papain results in generation of fragment antigen binding (Fab). Pepsin digestion of IgG results in fragment crystallisable (fc), comprises the H chain constant region. Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection. IgG antibody have enormous therapeutic potential and the Fc region is involved in the development of therapeutic antibody.
IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative

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)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Development of a particle concentration fluorescence immunoassay for the quantitative determination of IgG in bovine milk
Losso JN et al
Journal of Agricultural and Food Chemistry, 41, 682-686 (1993)
Structure and function of immunoglobulins
Schroeder Jr HW and Cavacini L
The Journal of Allergy and Clinical Immunology, 125, S41-S52 (2010)
Francesca Martini et al.
Nature communications, 10(1), 75-75 (2019-01-10)
The canine heartworm (Dirofilaria immitis) is a mosquito-borne parasitic nematode whose range is extending due to climate change. In a four-dimensional analysis involving HPLC, MALDI-TOF-MS and MS/MS in combination with chemical and enzymatic digestions, we here reveal an N-glycome of
Molecular properties of human IgG subclasses and their implications for designing therapeutic monoclonal antibodies against infectious diseases
Irani V, et al.
Molecular Immunology, 67 (2015)
Structure and function of immunoglobulins.
Schroeder Jr H W and Cavacini L
The Journal of Allergy and Clinical Immunology, 125(2), S41-S52 (2010)

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