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P9787

Sigma-Aldrich

Anti-Goat IgG (whole molecule)−R-Phycoerythrin antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Rabbit Anti-Goat IgG (whole molecule)−R-PE

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0.25 ML
R$ 2.722,00

R$ 2.722,00


Previsão de entrega em12 de abril de 2025


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0.25 ML
R$ 2.722,00

About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.46

R$ 2.722,00


Previsão de entrega em12 de abril de 2025


Solicite uma grande encomenda

fonte biológica

rabbit

Nível de qualidade

conjugado

phycoerythrin (R-PE) conjugate

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

secondary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

condição de armazenamento

protect from light

técnica(s)

indirect immunofluorescence: 1:20

Condições de expedição

wet ice

temperatura de armazenamento

2-8°C

modificação pós-traducional do alvo

unmodified

Descrição geral

Immunoglobulins (Igs) belongs 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.
Primary goat antibodies are often used to study target proteins for various clinical and research purposes. Thus, secondary antibodies against goat IgGs can be used to facilitate the accurate detection and localization of target proteins. Specificity of anti-goat IgG (whole molecule) has been tested by immunoelectrophoresis versus goat serum and goat IgG, prior to conjugation with R-Phycoerythrin.

Imunogênio

Purified goat IgG

Aplicação

Anti-Goat IgG (whole molecule)-R-Phycoerythrin antibody is suitable for use in indirect immunofluorescence (1:20).
Anti-Goat IgG (whole molecule)−R-Phycoerythrin antibody produced in rabbit has been used in immunoassay.

Ações bioquímicas/fisiológicas

Pepsin digestion of IgG results in fragment crystallisable (fc), with a H chain constant region. Papain digestion of IgG generates fragment antigen binding (Fab) with one complete light(L) chain and a variable and CH1 region of heavy(H) chain. IgG antibody have enormous therapeutic potential. Deficiency of IgG1 results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions. IgG4 is associated with asymptomatic infection.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

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


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Lignin isolated from primary walls of hybrid aspen cell cultures indicates significant differences in lignin structure between primary and secondary cell wall
Christiernin M, et al.
Plant Physiology and Biochemistry, 43(8), 777-785 (2005)
Structure and function of immunoglobulins
Schroeder Jr HW and Cavacini L
The Journal of Allergy and Clinical Immunology, 125, S41-S52 (2010)
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)
Gestur Vidarsson et al.
Frontiers in immunology, 5, 520-520 (2014-11-05)
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These

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