IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins. Goat Anti-Rabbit IgG (whole molecule)-Alkaline Phosphatase antibody binds to all rabbit Igs.
Immunoglobulin G (IgG) is part of the immunoglobulin family and is widely expressed in the serum. It consists of a gamma (γ) heavy chain in the constant (C) region. The monomeric structure of IgG consists of two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity (Fab fragments). The third fragment known as fragment crystallizable (Fc).
Citrullination of antithrombin by PADI4 was analyzed by ELISA using alkaline phosphatase conjugated goat anti-rabbit IgG as the secondary diluted at 1:5000 in 0.05M carbonate/bicarbonate buffer (Ph 9.6).
Goat Anti-Rabbit IgG (whole molecule)-Alkaline Phosphatase antibody has been used for ELISA assays at a dilution of 1:5,000.
Protein expression in maize endosperm amyloplast preparations or whole cell lysates were analyzed by alkaline phosphatase-conjugated goat anti-rabbit IgG as the secondary antibody.
Physical form
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol, 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.
Proceedings of the National Academy of Sciences of the United States of America, 94(25), 13458-13462 (1998-02-12)
RNA polymerase I (Pol I) transcription in the yeast Saccharomyces cerevisiae is greatly stimulated in vivo and in vitro by the multiprotein complex, upstream activation factor (UAF). UAF binds tightly to the upstream element of the rDNA promoter, such that
The Biochemical journal, 282 ( Pt 2), 615-620 (1992-03-01)
Serum amyloid A protein (SAA), an acute-phase reactant and apolipoprotein of high-density lipoprotein, is a polymorphic protein with six reported isoforms. These are the products of three genes, i.e., cDNA pA1, cDNA pSAA82 and genomic DNA SAAg9, the last two
The extracytoplasmic function (ECF) σ factor, σE , is a key regulator of the cell envelope stress response in Streptomyces coelicolor. Although its role in maintaining cell wall integrity has been known for over a decade, a comprehensive analysis of
Journal of virology, 74(24), 11598-11607 (2000-11-23)
We describe an improved genetic immunization strategy for eliciting a full spectrum of anti-hepatitis C virus (HCV) envelope 2 (E2) glycoprotein responses in mammals through electrical gene transfer (EGT) of plasmid DNA into muscle fibers. Intramuscular injection of a plasmid
Frontiers in plant science, 3, 290-290 (2012-12-28)
The potato mop-top virus (PMTV) triple gene block 2 (TGB2) movement proteins fused to monomeric red fluorescent protein (mRFP-TGB2) was expressed under the control of the PMTV subgenomic promoter from a PMTV vector. The subcellular localizations and interactions of mRFP-TGB2
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.