B7139
Anti-Rat IgG (whole molecule)–Biotin antibody produced in goat
affinity isolated antibody, buffered aqueous solution
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biological source
goat
Quality Level
conjugate
biotin conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
technique(s)
direct ELISA: 1:20,000
storage temp.
2-8°C
target post-translational modification
unmodified
General description
IgGs are glycoprotein antibodies that modulate several immune responses. Rat IgGs have four subclasses, namely, IgG1, IgG2a, IgG2b, and IgG2c. Rat IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rat IgG is a useful tool for the analysis of target proteins
Anti-Rat IgG (whole molecule)-Biotin antibody binds to all rat immunoglobulins.
Anti-Rat IgG (whole molecule)-Biotin antibody binds to all rat immunoglobulins.
Immunogen
Purified rat IgG
Application
Anti-Rat IgG (whole molecule)-Biotin antibody is suitable for use in immunohistochemistry and sandwich ELISA.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Immunohistochemistry (1 paper)
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 Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Sanne S Berger et al.
PloS one, 8(7), e69117-e69117 (2013-07-23)
Members of the Plasmodium falciparum Erythrocyte Membrane protein 1 (PfEMP1) family expressed on the surface of malaria-infected erythrocytes mediate binding of the parasite to different receptors on the vascular lining. This process drives pathologies, and severe childhood malaria has been
J W Simecka et al.
Infection and immunity, 57(11), 3570-3575 (1989-11-01)
Chronic respiratory disease in rats, resulting from Mycoplasma pulmonis infection, is useful in the study of the immunological mechanisms in similar inflammatory diseases and provides a unique opportunity to study the interactions between systemic and mucosal immune systems in a
Francesco Alessandrini et al.
Oncogene, 38(23), 4467-4479 (2019-02-14)
Oncolytic herpes simplex viruses are proving to be effective in clinical trials against a number of cancers. Here, R-115, an oncolytic herpes simplex virus retargeted to human erbB-2, fully virulent in its target cells, and armed with murine interleukin-12 was
Maria A Usik et al.
International journal of molecular sciences, 22(17) (2021-09-11)
The effect of weightlessness on gametogenesis and the functional state of female germ cells are still poorly understood. We studied the ovaries of Drosophila melanogaster, the full development cycle of which (from zygote to sexually mature adults) passed under simulated
Tomomi Kurane et al.
Okajimas folia anatomica Japonica, 96(2), 49-56 (2020-01-07)
Embryo implantation is an immunologically paradoxical event. In humans and rodents, blastocysts adhere to uterine epithelium and then invade into endometrial stroma, while maternal body is protected from extraneous materials by its immune system. Eosinophils, a kind of leucocytes involving
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