RecombiMAb human IgG4 (S228P) isotype control, anti-hen egg lysozyme

Catalog #CP147
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$224.00 - $6,087.00

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  • 100 mg - $6,087.00
  • 50 mg - $4,356.00
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  • 1 mg - $224.00
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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.  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.


Isotype Human IgG4, κ
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/μg)
Determined by LAL gel clotting assay
Aggregation <5%
Determined by SEC
Purity >95%
Determined by SDS-PAGE
Sterility 0.2 µm 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
Theiler’s Murine Encephalomyelitis: Negative
Storage The antibody solution should be stored at the stock concentration at 4°C. Do not freeze.
    • 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.


    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 Fcγ-receptors (FcγR). Thus, choosing IgG subclasses, such as human IgG4, with a low ability to interact with FcγRs has been identified as a potential strategy to limit FcγR or complement pathway dependent side-effects. However, even immunomodulatory antibodies on the human IgG4 background may interact with cellular FcγRs 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 © 2022 Reitinger, Ipsen-Escobedo, Hornung, Heger, Dudziak, Lux and Nimmerjahn.

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