€691.00 €587.35
Immunoglobulin G (IgG) is a member of the immunoglobulin superfamily of glycoproteins that plays a central role in the adaptive immune response.{53880,53882} It is produced by B cells and later secreted by plasma cells and is the most abundant circulating antibody in rabbit serum. IgG consists of two identical heavy chains of approximately 50 kDa each and two identical light chains of approximately 25 kDa each.{53880} The heavy chains are linked together by a single disulfide bond to form an Fc region and also combine with the light chains through additional disulfide bonds to form the Fab region, which mediate receptor and antigen binding, respectively. IgG is produced following IgM class-switching in response to infection and is involved in numerous humoral host defense responses, including antibody-dependent cell-mediated cytotoxicity (ADCC), toxin neutralization, and pathogen opsonization.{55170,53880,53883} Rabbits express three light chains, IgG? (K1), IgG? (K2), and IgG?, with IgG? (K1)-containing IgGs comprising approximately 90% of the total IgG population. Unlike human and mouse IgG, rabbit IgG has a single subclass and a short upper and middle hinge length of only 11 residues that facilitates the hinge extension necessary for binding of the Fc receptor (FcR) and activating complement component 1q (C1q) to facilitate complement activation.{53882,53880} Cayman’s IgG (rabbit) Monoclonal Antibody – Biotinylated can be used for ELISA and Western blot (WB; non-reducing conditions) applications. The antibody recognizes the Fab region of IgG at approximately 150 kDa from rabbit samples.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 50 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Host | Goat |
| Antigen | Rabbit IgG |
| Clone | RMG01 |
| Isotype | IgG |
| Application(s) | ELISA, WB (non-reducing conditions) |
| Formulation | 50 µg of protein G-affinity purified monoclonal antibody |
| Custom code | 3822.19 |
| UNSPSC code | 12352203 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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