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A7289

Sigma-Aldrich

Anti-Guinea Pig IgG (whole molecule)−Peroxidase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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About This Item

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

biological source

goat

conjugate

peroxidase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:10,000

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Related Categories

General description

IgG consists of four sub-classes, like IgG1, IgG2, IgG3, and IgG4. IgG is composed of four polypeptide chains-two heavy chains (γ chains) and two light chains (κ or λ chains) which are linked by inter-chain disulfide bonds. The heavy chains consist of a N-terminal variable domain (VH) and three constant domains (CH1, CH2, CH3). A hinge region exists between the CH1 and CH2 region. The light chains have one N-terminal variable domain (VL) and one constant domain (CL).

Immunogen

Purified guinea pig IgG

Application

Anti-H. pylori IgGs in guinea pig sera was measured by ELISA using HRP-conjugated goat anti-guinea pig IgG (A 7289) at a dilution of 1:2000 in 1% BSA/PBS for 1 hour at 37°C.
Anti-Guinea Pig IgG (whole molecule)-Peroxidase antibody is suitable for use in immunocytochemistry and ELISA.

Biochem/physiol Actions

Guinea pig IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-guinea pig IgGs conjugated to detectable substrates are useful tools for the analysis of target proteins. Anti-Guinea Pig IgG (whole molecule)-Peroxidase antibody is specific for guinea pig IgG.
IgGs are glycoprotein antibodies that modulate several immune responses. It plays a major role in providing immunity to the infant from the mother via the placenta. IgG activates the complement system and regulates the antibody-dependent cell-mediated cytotoxicity (ADCC).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin with preservative.

Preparation Note

Antiserum is developed in goat using purified guinea pig IgG as the immunogen. Antibody is isolated from goat anti-guinea pig IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins that do not specifically bind to guinea pig IgG. Goat anti-guinea pig IgG is conjugated to Sigma Horseradish Peroxidase, Type VI (Product No. P 8375) by a modification of the periodate method of Wilson and Nakane.

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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Pictograms

Exclamation markEnvironment

Signal Word

Warning

Hazard Statements

Hazard Classifications

Aquatic Chronic 2 - Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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X X Zhu et al.
Experimental & applied acarology, 13(2), 153-159 (1991-12-11)
Immunocytochemical staining based on the peroxidase-antiperoxidase method has shown that some neurosecretory cells (NSC) in the synganglion of the adult female tick Ornithodoros parkeri react with an antibody to bovine insulin. There are 18 regions of paraldehyde fuchsin-positive NSC of
Experimental Helicobacter pylori Infection Induces Antral Gastritis and Gastric Mucosa-Associated Lymphoid Tissue in Guinea Pigs.
Shomer, N.
Infection and Immunity, 66, 2647-2618 (1998)
IgG placental transfer in healthy and pathological pregnancies
Palmeira P, et al.
Clinical & Developmental Immunology, 2012 (2011)
Carolin Massalski et al.
PloS one, 10(3), e0115832-e0115832 (2015-03-31)
The Arabidopsis E-NTPDase (ecto-nucleoside triphosphate diphosphohydrolase) AtAPY1 was previously shown to be involved in growth and development, pollen germination and stress responses. It was proposed to perform these functions through regulation of extracellular ATP signals. However, a GFP-tagged version was
P D Fisher et al.
Gene therapy, 24(12), 757-767 (2017-11-07)
DNA vaccines delivered using electroporation (EP) have had clinical success, but these EP methods generally utilize invasive needle electrodes. Here, we demonstrate the delivery and immunogenicity of a DNA vaccine into subcutaneous adipose tissue cells using noninvasive EP. Using finite

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