Anti-Goat IgG (whole molecule)–Peroxidase antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Anti Goat Igg, Anti-Goat IgG (whole molecule)–Peroxidase antibody produced in rabbit
MDL number:
Pricing and availability is not currently available.

biological source


Quality Level

antibody form

affinity isolated antibody

antibody product type

secondary antibodies




buffered aqueous solution

species reactivity



direct ELISA: 1:40,000
dot blot: 1:80,000-1:160,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200


peroxidase conjugate

shipped in

dry ice

storage temp.


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General description

Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. An immunoglobulin has two heavy chain and two light chain connected by disulfide bond. It is a glycoprotein and a major class of immunoglobulin. Goat IgG has two subclasses- IgG1 and IgG2.
Goat IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-goat IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins. Rabbit anti-goat IgG (whole molecule)-peroxidase antibody binds to all goat Igs.


Specificity of Anti-Goat IgG- Peroxidase is determined by immunoelectrophoresis (IEP) versus normal goat serum and goat IgG.


Purified goat IgG


LNCAP cell lysates were analyzed by western blot using HRP conjugated rabbit anti-goat IgG as the secondary at a 1:7500 dilution in TBSt for 1 hour at room temperature.
Rabbit Anti-Goat IgG (whole molecule)-Peroxidase antibody has been used for immunoblotting assays. The antibody can also be used for direct ELISA (1:40,000), dot blot (1:80,000-1:160,000) and immunohistochemistry (1:200) assays.
Anti-Goat IgG (whole molecule)–Peroxidase antibody has been used in
  • western blotting
  • immunohistochemical and immunofluorescent analysis
  • visualization of cross-reactivity
  • protein analysis
  • indirect ELISA for detection of specific IgG against C. pseudotuberculosis
  • immunoprecipitation (IP)

Biochem/physiol Actions

Immunoglobulin G (IgG) glycoprotein antibodies modulates several immune responses. It mainly participates in hypersensitivity type II and type III.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing, or storage in "frost-free" freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.


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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Signal Word


Hazard Statements


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding.
Hartmann J, et al.
The Journal of Biological Chemistry, jbc-M111 (2012)
Suppression of thrombospondin 1 and 2 production by herpes simplex virus 1 infection in cultured keratocytes.
Choudhary A, et al.
Molecular Vision, 11, 163-168 (2005)
Properdin plays a protective role in polymicrobial septic peritonitis.
Stover C M, et al.
Journal of Immunology, 180(5), 3313-3318 (2008)
Evaluation of the humoral and cellular immune response to different antigens of Corynebacterium pseudotuberculosis in Caninde goats and their potential protection against caseous lymphadenitis.
Moura-Costa L F, et al.
Veterinary Immunology and Immunopathology, 126(1-2), 131-141 (2008)
James W G.
Monoclonal Antibodies: Principles and Practice (1996)

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