RecombiMAb human IgG4 (S228P) isotype control, anti-hen egg lysozyme
Product Details
This human IgG4 S228P isotype control antibody reacts with hen egg lysozyme and has low or no specific binding to any human sample.Ā The S228P mutation is included to prevent IgG4 Fab exchange. This is a recombinant human IgG4 antibody produced in CHO cells.Note: This product was previously sold as catalog number BE0349 and is identical to the product previously sold as BE0349.
Specifications
Isotype | Human IgG4, Īŗ |
---|---|
Recommended Dilution Buffer | InVivoPure pH 7.0 Dilution Buffer |
Conjugation | This product is unconjugated. Conjugation is available via our Antibody Conjugation Services. |
Mutations | S228P |
Immunogen | Hen egg lysozyme (HEL) |
Formulation |
PBS, pH 7.0 Contains no stabilizers or preservatives |
Endotoxin |
<1EU/mg (<0.001EU/Ī¼g) Determined by LAL gel clotting assay |
Aggregation |
<5% Determined by SEC |
Purity |
>95% Determined by SDS-PAGE |
Sterility | 0.2 Āµm filtration |
Production | Purified from CHO cell supernatant in an animal-free facility |
Purification | Protein A |
RRID | AB_2894768 |
Molecular Weight | 150 kDa |
Murine Pathogen Tests |
Ectromelia/Mousepox Virus: Negative Hantavirus: Negative K Virus: Negative Lactate Dehydrogenase-Elevating Virus: Negative Lymphocytic Choriomeningitis virus: Negative Mouse Adenovirus: Negative Mouse Cytomegalovirus: Negative Mouse Hepatitis Virus: Negative Mouse Minute Virus: Negative Mouse Norovirus: Negative Mouse Parvovirus: Negative Mouse Rotavirus: Negative Mycoplasma Pulmonis: Negative Pneumonia Virus of Mice: Negative Polyoma Virus: Negative Reovirus Screen: Negative Sendai Virus: Negative Theilerās Murine Encephalomyelitis: Negative |
Storage | The antibody solution should be stored at the stock concentration at 4Ā°C. Do not freeze. |
Additional Formats
Recommended Products
- Immunology and Microbiology,
Modulation of urelumab glycosylation separates immune stimulatory activity from organ toxicity.
In Frontiers in Immunology on 18 October 2022 by Reitinger, C., Ipsen-Escobedo, A., et al.
PubMed
Checkpoint control and immunomodulatory antibodies have become important tools for modulating tumor or self-reactive immune responses. A major issue preventing to make full use of the potential of these immunomodulatory antibodies are the severe side-effects, ranging from systemic cytokine release syndrome to organ-specific toxicities. The IgG Fc-portion has been demonstrated to contribute to both, the desired as well as the undesired antibody activities of checkpoint control and immunomodulatory antibodies via binding to cellular FcĪ³-receptors (FcĪ³R). Thus, choosing IgG subclasses, such as human IgG4, with a low ability to interact with FcĪ³Rs has been identified as a potential strategy to limit FcĪ³R or complement pathway dependent side-effects. However, even immunomodulatory antibodies on the human IgG4 background may interact with cellular FcĪ³Rs and show dose limiting toxicities. By using a humanized mouse model allowing to study the immunomodulatory activity of human checkpoint control antibodies in vivo, we demonstrate that deglycosylation of the CD137-specific IgG4 antibody urelumab results in an amelioration of liver toxicity, while maintaining T cell stimulatory activity. In addition, our results emphasize that antibody dosing impacts the separation of side-effects of urelumab from its therapeutic activity via IgG deglycosylation. Thus, glycoengineering of human IgG4 antibodies may be a possible approach to limit collateral damage by immunomodulatory antibodies and allow for a greater therapeutic window of opportunity. Copyright Ā© 2022 Reitinger, Ipsen-Escobedo, Hornung, Heger, Dudziak, Lux and Nimmerjahn.