Goat anti-Hamster IgG (H+L) Secondary Antibody [Janelia Fluor 549] Summary
This Goat anti-Hamster IgG (H+L) Secondary Antibody (Pre-adsorbed) was developed against Armenian and Golden Syrian Hamster IgG, whole molecule.
This antibody was pre-adsorbed against Mouse and Rat Serum Proteins.
No reaction was observed against Mouse or Rat Serum Proteins. This antibody will react with heavy chains of Golden Syrian & Armenian Hamster IgG and with light chains of most Golden Syrian & Armenian Hamster immunoglobulins.
- ELISA 1:100-1:2000
- Immunocytochemistry/Immunofluorescence 1:10-1:500
- Immunohistochemistry 1:10-1:500
- Western Blot 1:100-1:2000
Optimal dilution of this antibody should be experimentally determined.
Cricetulus migratorius (Armenian Hamster); Melanochromis auratus (Golden Syrian Hamster)
Packaging, Storage & Formulations
Store at 4C in the dark.
50mM Sodium Borate
0.05% Sodium Azide
Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.
Antibodies, also known as immunoglobulins (Igs) are critical for immunity and are grouped into five primary classes: IgG, IgM, IgA, IgD, and IgE. The most abundant antibody isotype is immunoglobulin G (IgG) with concentrations ranging from 7.5-22 mg/ml in human serum and has a molecular weight of 150 kDa. The major effector functions of IgG include neutralization, opsonization, complement fixation and antibody dependent cell-mediated cytotoxicity (ADCC). This monomeric immunoglobulin, expressed on the surface of mature B cells, is often depicted as a Y-shape and comprised of 2 heavy chains and 2 light chains linked by disulfide bonds. The heavy chain is type gamma including subtypes gamma 1, gamma 2, gamma 3, and gamma 4 while the light chain is either a kappa or lambda chain. An IgG molecule has two antigen binding sites, each consisting of a heavy and light chain N-terminal variable domain. When combined with the constant heavy chain 1 (Ch1) and the constant light chain domains, it forms the fragment antigen-binding (Fab) region (2 per antibody). The remaining domains (Ch2-Ch4) of both heavy chains make up the Fc region and contain a site for covalently linking an enzymatic or fluorochrome probe, such as HRP or Janelia Fluor 549, for target detection and visualization (1,2,3).
The 4 IgG subclasses, sharing 95% amino acid identity, include IgG1, IgG2, IgG3, and IgG4 for humans and IgG1, IgG2a, IgG2b, and IgG3 for mice. The relative abundance of each human subclass is 60% for IgG1, 32% for IgG2, 4% for IgG3, and 4% for IgG4. In an IgG deficiency, there may be a shortage of one or more subclasses (4).
1. Painter RH. (1998) Encyclopedia of Immunology (Second Edition). Elsevier. 1208-1211
2. Chapter 9 - Antibodies. (2012) Immunology for Pharmacy. Mosby 70-78
3. Schroeder H, Cavacini, L. (2010) Structure and Function of Immunoglobulins. J Allergy Clin Immunol. 125(2 0 2): S41-S52. PMID: 20176268
4. Vidarsson G, Dekkers G, Rispens T. (2014) IgG subclasses and allotypes: from structure to effector functions. Front Immunol. 5:520. PMID: 25368619
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Secondary Antibodies are guaranteed
for 1 year from date of receipt.
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