Goat anti-Ferret IgG (H+L) Secondary Antibody [HRP]

• Reactivity: Ma
• Applications: WB, ELISA, ICC/IF, IHC
• Clonality: Polyclonal
• Host: Goat
• Conjugate: HRP
• Concentration: 1.0 mg/ml

Goat anti-Ferret IgG (H+L) Secondary Antibody [HRP] Summary

• Immunogen: This Goat anti-Ferret IgG (H+L) Secondary Antibody [HRP] was developed against ferret IgG-heavy and light chain.
• Specificity: By immunoelectrophoresis and ELISA this Goat anti-Ferret IgG (H+L) Secondary Antibody [HRP] reacts specifically with ferret IgG and with light chains common to other ferret immunoglobulins. No 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 1:10000-1:100000
  • Immunocytochemistry/ Immunofluorescence 1:200 - 1:5000
  • Immunohistochemistry 1:200 - 1:5000
  • Immunohistochemistry-Paraffin
  • Western Blot 1:5000-1:50000
• Readout System:
  • NovaLume Plus Chemiluminescent Reagent LUM-555

Packaging, Storage & Formulations

• Storage: Store at 4C. Do not freeze.
• Buffer: Phosphate Buffered Saline (PBS) containing 0.2% BSA
• Preservative: 0.05% Pro-Clean 400
• Concentration: 1.0 mg/ml
• Purity: Immunogen affinity purified

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.

Publications for IgG (H+L) Antibody (NB7224)(8)

Publications using NB7224

• Wang W, Sayedahmed E, Alhashimi M et al. A bovine adenoviral-vector-based universal influenza vaccine confers protection against influenza A and B viruses in mice and ferrets Molecular Therapy. Nucleic Acids 2025-09-09 [PMID: 40635672]
• Leonard RA, Burke KN, Spreng RL et al. Improved influenza vaccine responses after expression of multiple viral glycoproteins from a single mRNA Nature Communications 2024-10-08 [PMID: 39379405]
• Chiba S, Kong H, Neumann G, Kawaoka Y Influenza H3 hemagglutinin vaccine with scrambled immunodominant epitopes elicits antibodies directed toward immunosubdominant head epitopes mBio 2023-07-19 [PMID: 37466314] (ELISA)
  
  Details:
  1:10,000 dilution in PBS-BT
• Bewley KR, Gooch K, Thomas KM Et al. Immunological and pathological outcomes of SARS-CoV-2 challenge following formalin-inactivated vaccine in ferrets and rhesus macaques Sci Adv 2021-09-13 [PMID: 34516768] (ELISA)
  
  Details:
  Citation using the HRP version of this antibody.
• Ryan KA, Bewley KR, Fotheringham SA, et al Dose-dependent response to infection with SARS-CoV-2 in the ferret model and evidence of protective immunity Nat Commun 2021-01-05 [PMID: 33398055] (ELISA)
  
  Details:
  Citation using the HRP version of this antibody.
• Zalewski A, Virtanen JME, Brzezinski M et al. Aleutian mink disease: spatio-temporal variation of prevalence and influence on the feral American mink Transbound Emerg Dis 2020-11-16 [PMID: 33197283] (ELISA)
• Wong SS, Kaplan B, Zanin M et al. Impact of adjuvants on the immunogenicity and efficacy of split-virion H7N9 vaccine in ferrets J. Infect Immun. [PMID: 25712975] (ELISA)
  
  Details:
  Citation using the HRP form of this antibody.
• Silin D, Lyubomska O, Ludlow M et al. Development of a challenge-protective vaccine concept by modification of the viral RNA-dependent RNA polymerase of canine distemper virus. J Virol. [PMID: 17898047]
  
  Details:
  Citation using the HRP form of this antibody.