Goat anti-Bat IgG (H+L) Secondary Antibody [DyLight 488] Summary
Immunogen |
This Goat anti-Bat IgG (H+L) Secondary Antibody was developed against bat IgG-heavy and light chain. |
Specificity |
By immunoelectrophoresis and ELISA this Goat anti-Bat IgG (H+L) Secondary Antibody reacts specifically with Bat IgG and with light chains common to other Bat immunoglobulins. Antibody has been shown to react with bat genus species Pteropus vampirus, Desmodus rotundus, Eptesicus fuscus, Tadrida pumila, T. condylura, Hypsignathus monstrosus, Rosettus aegyptiacus, Epomorphus crypturus, Molossus species. And Phylostomus species. No antibody was detected against non-immunoglobulin serum proteins. This may cross react with IgG from other species. |
Isotype |
IgG |
Clonality |
Polyclonal |
Host |
Goat |
Purity |
Immunogen affinity purified |
Applications/Dilutions
Dilutions |
- ELISA
- Flow Cytometry
- Immunocytochemistry/ Immunofluorescence
- Immunohistochemistry
- Immunohistochemistry-Paraffin
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
50mM Sodium Borate |
Preservative |
0.05% Sodium Azide |
Purity |
Immunogen affinity purified |
Notes
DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Background
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).
References
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
Limitations
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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