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P9787

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Synonym(s):

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

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

phycoerythrin (R-PE) conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

storage condition

protect from light

technique(s)

indirect immunofluorescence: 1:20

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

General description

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.

Immunogen

Purified goat IgG

Application

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.

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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