Proteins with Enhanced Activity & Stability

AdipoGen Life Sciences specializes in the development of recombinant proteins that show enhanced activity and stability, produced in mammalian cells. 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.

The development of recombinant proteins is performed using different production expression systems, including the mammalian cell lines CHO and HEK 293. The mammalian cell lines allow AdipoGen Life Sciences to produce exogenous recombinant proteins secreted into the cell medium with post-translational modifications and glycosylations closer to endogenous proteins compared to productions in E. coli. However, for some difficult-to-produce in mammalian cells proteins, we also use bacteria (E. coli) and/or insect cells as a host. AdipoGen Life Sciences’ first goal is to provide high purity, low endotoxin and biologically active recombinant proteins, leveraging its in-house protein technologies.

Recombinant proteins are used throughout the life science academia and industry in a plethora of applications. They elicit their mechanism of action by activating signaling pathways through binding to specific cell-surface receptors. Their use ranges from cell culture to bioprocessing and advanced cell and gene therapy. A defined composition of the cell culture medium to guarantee batch-to-batch reproducibility has become inevitable. The development of animal-component-free recombinant proteins eliminates the risk of contamination that has been associated with animal and human serum-derived media.

AdipoGen Life Sciences' initiative to implement the production in serum-free (animal-component free) media conditions, copes with the need for its highly biologically active and stable proteins for these newly emerging markets and helps advance life sciences research. Ask for serum-free production lots!

Product Group Overview

TNF Ligands Multimeric Proteins

  • 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).
  • MultimericLigands™ are constructs in which two trimeric TNFSF ligands are linked via the oligomeric collagen domain of Adiponectin [ACRP30headless].
  • MultimericLigands™ mimic the membrane-bound forms of the proteins and show high activity.
  • For in vitro studies!

For selected Products please see below or the full panel of Multimeric Proteins.
Multimeric Proteins

Product Name PID Host Species Activity
CD40L (human) (multimeric) (rec.) AG-40B-0010 CHO cells Human

Potent B cell and T cell expansion tool for Cell Therapy Application.

Accelerates ex-vivo TIL expansion for Immunotherapy.

NEW CD40L (human) (multimeric) (rec.) (Certified Serum Grade) AG-40B-0010CSG CHO cells Human

Potent B cell and T cell expansion tool for Cell Therapy Application.

Accelerates ex-vivo TIL expansion for Immunotherapy.

CD40L (mouse) (multimeric) (rec.) AG-40B-0020 CHO cells Human, Mouse Potent B cell expansion tool.
FasL (human) (multimeric) (rec.) AG-40B-0130 HEK 293 cells Human, Mouse Potent apoptosis Inducer in human Jurkat T cells.
TNF-α (human) (multimeric) (rec.) AG-40B-0019 HEK 293 cells Human, Mouse Activates human and mouse TNF-R1 and TNF-R2.

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COMP-Fusion Proteins - Improved Avidity & Biological Activity

  • The avidity (binding) and activity of selected proteins are improved by the addition of an oligomerization domain fused at the N- or C-terminus of the protein of interest.
  • 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.
  • For in vitro and in vivo studies!

COMP Proteins

Product Name PID Host Species
COMP (rat):Angiopoietin-1 (human) (rec.) AG-40B-0147 CHO cells Human
VISTA (mouse):COMP (mouse) (rec.) (His) AG-40B-0181 HEK 293 cells Mouse
VISTA (human):COMP (mouse) (rec.) (His) AG-40B-0183 HEK 293 cells Human

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Monomeric Proteins fused to Fc (KIH-Technology)

  • The knobs-into-holes (KIH) strategy is a pioneering format, permitting heavy-chain heterodimerization to create an “IgG with two different arms”.
  • The KIH technology can also be used for protein engineering.
  • AdipoGen Life Sciences developed various interleukins (e.g. IL-2, IL-33 and IL-38) into an Fc-fusion protein using the KIH technology.
  • The KIH proteins are monomeric (see Figure) with greatly enhanced stability and substantially improved pharmacokinetics (PK) while maintaining cytokine activity.
  • AdipoGen Life Sciences also developed heterodimeric proteins using the KIH-technology.
  • These special monomeric Fc-constructs are produced in mammalian cells with low endotoxin content.
  • For in vitro and in vivo studies!

Knobs-into-Holes (KIH) Technology:
Lit: J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)
Monomeric Proteins

  • The monomeric IL-2 proteins, including the IL-2 (human) (monomeric):Fc-KIH (human) (rec.) (#AG-40B-0224), IL-2 (mouse) (monomeric):Fc-KIH (human) (rec.) (#AG-40B-0225) and IL-2 Superkine (monomeric):Fc-KIH (human) (rec.) (#AG-40B-0222) are activity tested and compared to a dimeric Fc fusion protein IL-2 Superkine (Fc) (#AG-40B-0111), all produced in mammalian cells with low endotoxin content. Activation of IL-2R is analyzed using the IL-2 Bioassay from Promega (#JA2201) consisting of a genetically engineered cell line expressing the IL-2R. When IL-2 binds to its receptor (IL-2R), receptor-mediated pathway signaling induces luminescence that is measured with a luminometer. The experiment shows a several-fold increased activity of the monomeric constructs.
Monomeric Proteins Activity

Product Name PID Host Species
IL-2 (human) (monomeric):Fc-KIH (human) (rec.) AG-40B-0224 HEK 293 cells Human, (Mouse)
IL-2 (mouse) (monomeric):Fc-KIH (human) (rec.) AG-40B-0225 HEK 293 cells Mouse, (Human)
IL-2 Superkine (monomeric):Fc-KIH (human) (rec.) AG-40B-0222 HEK 293 cells Human, Mouse
IL-2 Superkine H9T (monomeric):Fc-KIH (human) (rec.) AG-40B-0223 HEK 293 cells Human, Mouse
NEW IL-2 (human) (Switch-2) (monomeric):Fc-KIH (human) (rec.) AG-40B-0234 HEK 293 cells Human, Mouse
NEW IL-7 (human) (monomeric):Fc-KIH (human) (rec.) AG-40B-0238 HEK 293 cells Human, Mouse
NEW IL-23 (mouse):Fc-KIH (human) (rec.) AG-40B-0235 CHO cells Human, Mouse
NEW IL-27 (mouse):Fc-KIH (human) (rec.) AG-40B-0236 CHO cells Human, Mouse
NEW IL-33 (oxidation resistant) (human) (monomeric):Fc-KIH (human) (rec.) AG-40B-0233 HEK 293 cells Human, Mouse
IL-38 (aa 20-152) (human) (monomeric):Fc-KIH (human) (rec.) AG-40B-0226 HEK 293 cells Human
IL-38 (aa 3-152) (mouse) (monomeric):Fc-KIH (human) (rec.) AG-40B-0227 HEK 293 cells Mouse
IL-37 (human) (monomeric):Fc-KIH (human) (rec.) AG-40B-0221 HEK 293 cells Human, Mouse
Fc-KIH (human) IgG1 Control (rec.) AG-35B-0015 HEK 293 cells Control for Human, Mouse

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Fc-Fusion Proteins (wild-type or non-lytic)

  • Fc-Fusion proteins (also known as Fc-Chimeric Fusion proteins, Ig-based Chimeric Fusion proteins and Fc-tag proteins) are composed of the Fc domain of IgG genetically linked to a protein of interest. Dimeric structures are formed during the production in mammalian cells.
  • The fusion of a cytokine sequence to the Fc domain of an IgG (human or mouse) determines a prolonged circulating half-life time 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: 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).
  • For in vitro and especially in vivo studies!

Fc Fusion Proteins

Product Name PID Host Species
LAG-3 (human):Fc (human) (rec.) AG-40B-0031 CHO cells Human, Monkey, Mouse
LAG-3 (mouse):Fc (mouse) (rec.) AG-40B-0039 CHO cells Human, Mouse
CTLA-4 (human):Fc (human) (rec.) (non-lytic) CHI-HF-220A4 CHO cells Human
CTLA-4 (mouse):Fc (mouse) (rec.) (non-lytic) CHI-MF-120A4 NS1 cells Mouse
IL-21 (mouse):Fc (mouse) (rec.) (non-lytic) CHI-MF-12021 CHO cells Mouse
IL-35 (human):Fc (human) (rec.) CHI-HF-21035 CHO cells Human
IL-35 (mouse):Fc (human) (rec.) CHI-MF-11135 CHO cells Mouse
Jagged-1 (mouse):Fc (human) (rec.) AG-40A-0157T HEK 293 cells Mouse
NEW VSTM5 (human):Fc (human) (rec.) (non-lytic) AG-40B-0237 HEK 293 cells Human
Browse More:
All AdipoGen Life Sciences Fc Fusion Proteins
All Chimerigen Fc Fusion Proteins
All Chimerigen Non-Lytic Fc Fusion Proteins
All Ancell Fc Fusion Proteins

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Proteins with Site-directed Mutations

Site-directed mutagenesis is a valuable tool to modify genes and study the structural and functional properties of a protein, based on the structure, function, catalytic mechanism and catalytic residues of enzymes and therefore of high importance for protein engineering. The mutation may be a single base change (point mutation), multiple base changes (many mutations), deletion or insertion.

Product Name PID Species Protein Improvements
DLL4 (human):Fc (human) (rec.) (highly active mutant) AG-40B-0176 Human, Mouse Several proprietary mutations result in a >20-fold increase in affinity relative to WT DLL4.
IL-2 Superkine (Fc) AG-40B-0111 Human, Mouse Mutations L80F / R81D / L85V / I86V / I92F are located in the molecule's core which acts to stabilize the structure and give it a receptor-binding conformation mimicking native IL-2 bound to CD25. These mutations effectively eliminate the functional requirement of IL-2 for CD25 expression and elicit the proliferation of T cells.
IL-2 Superkine (Fc) (H9T) AG-40B-0219 Human, Mouse A new version of IL-2 Superkine with an additional mutation Q126T reduces the binding of IL-2Rγ and promotes the expansion of CD8+ T cells without driving terminal differentiation.
IL-15 (mutant) (human):Fc (human) (rec.) CHI-HF-21015M Human Mutations at Q149D and Q156D make this protein specifically bind to the IL-15R, competitively inhibiting IL-15-triggered cell proliferation, promoting transplant tolerance and does not activate the STAT-signaling pathway.
IL-33 (oxidation resistant) (human) (rec.) (untagged) AG-40B-0160 Human, Mouse Amino acids 208 and 232 are mutated from cysteines to serines to protect IL-33 from oxidation.
TGFβ1 (mutant) (human):Fc (human) (rec.) CHI-HF-210TGFBM Human, Mouse Amino acids 33, 223, and 225 were mutated from cysteines into serines. This specific mutant protein containing the LAP+TGF-β1 domains allows the protein to be active.

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Selected Other Specialty Proteins

AdipoGen Life Sciences' R&D department has established in-house protocols for certain specialty proteins. These proteins have a special structure, multimerization or no tags. Only due to these special production protocols do these proteins elicit their biological activity. A few examples are listed below. A complete list of Untagged Proteins is available through the link.

Product Name PID Host Species
BAFF, Soluble (human) (60-mer) (rec.) (highly active) AG-40B-0112 E. coli Human, Mouse
NEW CD152 [CTLA-4] (human) (rec.) (untagged) AG-40B-0232 HEK 293 cells Human
Irisin (rec.) (untagged) (E. coli) AG-40B-0103 E. coli Human, Mouse
Progranulin (human) (rec.) (untagged) AG-40A-0188Y HEK 293 cells Human

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