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A3438

Sigma-Aldrich

Anti-Mouse IgG (γ-chain specific)−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Goat Anti-Mouse IgG (γ-chain specific)−AP

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About This Item

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

biological source

goat

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

mouse

technique(s)

direct ELISA: 1:30,000
dot blot: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

Immunoglobulin G (IgG) is a glycoprotein antibody that regulates immune responses such as phagocytosis and is also involved in the development of autoimmune diseases . Mouse IgGs have four distinct isotypes, namely, IgG1, IgG2a, IgG2b, and IgG3. IgG1 regulates complement fixation in mice . Anti-Mouse IgG (γ-chain specific)-Alkaline Phosphatase antibody is specific for mouse IgG when tested against purified mouse IgA, IgG and IgM myeloma proteins.

Immunogen

Purified mouse IgG.

Application

Anti-Mouse IgG (γ-chain specific)-Alkaline Phosphatase antibody is suitable for use in ELISA (1:1000) and western blot (1:2000). The product can also be used in immunohistochemistry (at 1:50 dilutions using formalin-fixed, paraffin-embedded sections).
Antibodies to Trypanosoma cruzi were detected in the sera of infected mice by ELISA with an alkaline phosphatase conjugated goat anti-mouse IgG chain specific. Plates were coated with T. cruzi antigen and blocked with 1% BSA/PBS prior to incubation with conjugated antibody.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
For use as secondary antibody in immuno-based assays.

Biochem/physiol Actions

Digestion of IgG by papain results in generation of fragment antigen binding (Fab) comprising of one complete L chain and a variable and CH1 region of H chain. Pepsin digestion of IgG results in fragment crystallizable (fc), comprises of the H chain constant region. IgG is abundant immunoglobulin in proteins in human serum. The four classes of IgG can be IgG1, IgG2, IgG3, and IgG4. IgG antibody has enormous therapeutic potential and the Fc are is for the development of therapeutic antibody.

Physical form

Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 10 mM glycine, 1 mM MgCl2, 50% glycerol, and 15 mM sodium azide.

Preparation Note

Affinity isolated antibody is obtained from anti-mouse IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the -chain of mouse IgG. Anti-Mouse IgG is conjugated to alkaline phosphatase by protein cross linking with 0.2% glutaraldehyde.

Analysis Note

ELISA was used to determine specificity of Anti-Mouse IgG (-chain specific)-Alkaline Phosphatase.The conjugate is specific for mouse IgG when tested against purified mouse IgA, IgG and IgM myeloma proteins.Immunoelectrophoresis (IEP) was used to establish antibody purity and identity prior to conjugation.Electrophoresis of the antibody preparation followed by diffusion versus anti-goat IgG and anti-goat whole serum results in single arcs of precipitation.

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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Regulatory Information

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Gonen A, et al.
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Generalized modules for membrane antigens (GMMA) represent a technology particularly attractive for designing affordable vaccines against Gram-negative bacteria. We explored such technology for the development of O-antigen-based vaccines against Shigella and nontyphoidal Salmonella. Adsorption of GMMA on Alhydrogel was required
F Micoli et al.
Vaccine, 29(4), 712-720 (2010-12-01)
An efficacious, low cost vaccine against typhoid fever, especially for young children, would make a major impact on disease burden in developing countries. The virulence capsular polysaccharide of Salmonella Typhi (Vi) coupled to recombinant mutant Pseudomonas aeruginosa exoprotein A (Vi-rEPA)
Li-Wen Chang et al.
PloS one, 8(12), e82916-e82916 (2013-12-18)
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The first layer of plant immunity is activated by cell surface receptor-like kinases (RLKs) and proteins (RLPs) that detect infectious pathogens. Constitutive interaction with the SUPPRESSOR OF BIR1 (SOBIR1) RLK contributes to RLP stability and kinase activity. As RLK activation

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