White Papers
Literature > White Papers > TGFbeta family
HumanKine® Authentic Recombinant Human TGFβ1 – Human Cell Expressed
Introduction
Cytokines are a group of proteins and polypeptides that organisms use as signaling molecules. Most cytokines are glycoproteins less than 30 kDa in size and bind to specific, high-affinity cell surface receptors. Due to their central role in the immune system, cytokines are involved in a variety of immunological, inflammatory and infectious diseases and widely used in research, diagnostics and therapeutics. Cytokines generally alter the gene expression pattern of the target cell which leads to changes in the rate of cell proliferation and/or in the state of cell differentiation. Currently, these proteins are predominantly produced in non-human cells (e.g. E. coli, SF9, CHO) and therefore lack authenticity due to the absence of physiologically relevant glycosylation. In addition, a number of important cytokines are not commercially available due to inadequate proteolytic processing, protein folding or other post-translational modifications that do not occur in the non-human cell expression systems.
HumanZyme has developed an efficient human-cell based technology, HumaXpress®, for scalable production of human cytokines. The company offers an expanding range of tag-free cytokines, including difficult-to-express protein members of the TGFß1 superfamily. HumanKine cytokines can be used as highly preferred reagents in a wide range of applications for cancer, inflammation, stem cell research, and antibody development.
TGFβ
Transforming growth factors beta (TGFß) are highly pleiotropic cytokines that act as cellular switches and regulate immune function, proliferation and epithelial-mesenchymal transition. These proteins are produced as precursors. A furin-like convertase processes the proprotein to generate an N-terminal latency-associated peptide (LAP) and a C-terminal mature TGFß. Disulfide-linked homodimers of LAP and TGFß remain non-covalently associated after secretion, forming the small latent TGFß complex that may interact with the extracellular matrix. Currently, commercially available TGFß proteins are produced in CHO cells. Due to the complex post-proteolytic modification, the yield is low and bulk volume is not readily available. HumanZyme has stably produced HumanKine TGFß1 from engineered human 293 cells. The protein is a disulfide-linked dimers of 25 kD that can be cost-effectively produced in large scale.
The bioactivity of HumanKine TGFß1 was determined by the dose-dependent inhibition of IL5 induced proliferation of human TF-1 cells. The results indicate HumanKine TGFß1 is 3-fold more active than the CHO expressed version.
(View more information for product number HZ-1011, HZ-1131, and HZ-1087. )
