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eTOPIX_Immune Proteins with Enhanced Activity & Stability – Sent on 30 June 2022
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eTOPIX Product Highlights - 30 June 2022 | www.adipogen.com | ||||||||||||||||||||
Immune Proteins with Enhanced Activity & Stability |
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AdipoGen Life Sciences specializes in the production of recombinant proteins in mammalian cells that show Enhanced Activity and Stability. Using proprietary in-house technologies together with established and published technologies, we engineer, develop and produce an innovative panel of recombinant proteins for different research fields including Cell Therapy Research. Better Solutions for in vivo and in vitro Research
NEW Monomeric Proteins fused to Fc (KIH-Technology)
AdipoGen Life Sciences developed various interleukins (e.g. IL-2, IL-37 and IL-38) into an Fc-fusion protein using the knobs-into-holes (KIH) technology. The final KIH proteins are monomeric with greatly enhanced stability and improved pharmacokinetics (PK) while maintaining the cytokine activity.
SELECTED PRODUCTS:
TNF Ligands Multimeric Proteins / MultimericLigands
Endogenous TNF superfamily ligands are either active as membrane-form (e.g. FasL, TRAIL, CD40L, OX40L) or are secreted and activated through oligomerization by the binding of proteoglycans at the surface of cells (e.g. APRIL).
SELECTED PRODUCTS:
MultimericLigands™ are constructs in which two trimeric TNFSF ligands are linked via the oligomeric collagen domain of Adiponectin [ACRP30headless], mimicking the natural membrane-assisted aggregation of natural ligands.
COMP-Fusion Proteins
COMP-Fusion Proteins are based on the pentamerization domain (minimal coiled-coil domain) of the cartilage oligomeric matrix protein (COMP), which is fused through a specific linker to proteins of interest. Using this technology AdipoGen Life Sciences generates cytokines with improved avidity and biological activity.
SELECTED PRODUCTS:
Fc-Fusion Proteins (wild-type or non-lytic)
The fusion of a cytokine sequence to the Fc domain of an IgG (human or mouse) determines a prolonged circulating half-life in vivo. The Fc domain folds independently and can improve the solubility and stability of the partner molecule both in vitro and in vivo. Non-lytic versions contain mutations to the complement (C1q) and FcgR I binding sites of the IgGs Fc fragment render the fusion proteins incapable of antibody-directed cytotoxicity (ADCC) and complement-directed cytotoxicity (CDC).
SELECTED PRODUCTS:
Custom Manufacturing & Bulk Quantities of Proteins with Enhanced Activity & Stability
Contact AdipoGen Life Sciences for custom manufacturing and bulk quantities of any protein using above indicated technologies.
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