Chimerigen - Immune Regulation Proteins. High Quality Fusion Proteins - Distributed in the UK & Ireland by Caltag Medsystems

Chimerigen

For many years Chimerigen Laboratories, LLC (Chimerigen) has developed, manufactured and marketed high quality and cutting edge proteins for biomedical and immunology research. A speciality of Chimerigen products is the production of unique immunoglobulin based chimeric fusion proteins using advanced cellular and molecular biological techniques. These reagents are used successfully in basic and applied research, providing advanced Immune Checkpoint Proteins, Interleukins and other Cytokines. Because of the high performance characteristics and quality the Chimerigen fusion proteins are widely recognized reagents and are cited in many scientific publications.

The collaboration between Chimerigen Laboratories and AdipoGen Life Sciences allows us to bring the Chimerigen product range to our UK & Ireland customers.

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  • Non-Lytic Fusion Proteins
  • IL-35 & Type 1 Diabetes
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Non-lytic Ig-based Chimeric Fusion Cytokines with Long Circulating Half-life

Chimerigen - Non-lytic Ig-based Chimeric Fusion Cytokines with Long Circulating Half-life
Figure: General structure of mouse non-lytic fusion proteins

The potential clinical application of cytokines to modulate immune responses is very high. Unfortunately, most cytokines have short circulating half-lives. Therefore, to facilitate the study of cytokine effects in vivo, a variety of non-lytic immunoglobulin-based chimeric cytokine fusion proteins have been created, in which a cytokine sequence has been genetically fused to the hinge, CH2 and CH3 regions of an immunoglobulin.

These non-lytic fusion proteins possess both the biological functions of the cytokine moiety and a prolonged circulating half-life determined by the Fc domain. They retain the potential to direct immune cytolytic mechanisms, antibody-dependent cell-mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) against cellular targets bound by the amino terminal binding moiety. These fusion molecules also have the promise of being minimally to negligibly immunogenic since they are made entirely from elements derived from the species to be treated.

Literature:

  • Localization of the binding site for the human high-affinity Fc receptor on IgG: A.R. Duncan, et al.; Nature 332, 563 (1988)
  • The binding site for Clq on IgG: A.R. Duncan & G. Winter; Nature 332, 738 (1988)
  • Administration of noncytolytic IL-10/Fc in murine models of lipopolysaccharide-induced septic shock and allogeneic islet transplantation: X.X. Zheng, et al.; J. Immunol. 154, 5590 (1995)

See all Non-Lytic Fusion Proteins

IL-35 & its Involvement in Type 1 Diabetes

Singh, et al. 2015, using Chimerigen’s IL-35 (mouse):Fc (human) (rec.) (CHI-MF-11135) as a key reagent, recently showed that circulating IL-35 levels were decreased in human Type 1 Diabetes (T1D) patients compared to healthy controls. The findings of this study suggest that insufficient IL-35 levels play a pivotal role in the development of T1D and that treatment with IL-35 should be investigated in the treatment of T1D and other autoimmune diseases.

Literature:

Interleukin-35 administration counteracts established murine type 1 diabetes – possible involvement of regulatory T cells: K. Singh, et al.; Sci. Rep. 5, ID12633 (2015)

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Documents

  Category Title  
Immune Regulation ProteinsImmunology DocumentsImmune Regulation Proteins  View
Immune Checkpoint Proteins, Interleukins & Cytokines  
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