InVitria

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Zhang D.,VENTRIA BIOSCIENCE | Nandi S.,VENTRIA BIOSCIENCE | Nandi S.,University of California at Davis | Bryan P.,VENTRIA BIOSCIENCE | And 5 more authors.
Protein Expression and Purification | Year: 2010

Transferrin is an essential ingredient used in cell culture media due to its crucial role in regulating cellular iron uptake, transport, and utilization. It is also a promising drug carrier used to increase a drug's therapeutic index via the unique transferrin receptor-mediated endocytosis pathway. Due to the high risk of contamination with blood-borne pathogens from the use of human or animal plasma-derived transferrin, recombinant transferrin is preferred for use as a replacement for native transferrin. We expressed recombinant human transferrin in rice (Oryza sativa L.) at a high level of 1% seed dry weight (10 g/kg). The recombinant human transferrin was able to be extracted with saline buffers and then purified by a one step anion exchange chromatographic process to greater than 95% purity. The rice-derived recombinant human transferrin was shown to be not only structurally similar to the native human transferrin, but also functionally the same as native transferrin in terms of reversible iron binding and promoting cell growth and productivity. These results indicate that rice-derived recombinant human transferrin should be a safe and low cost alternative to human or animal plasma-derived transferrin for use in cell culture-based biopharmaceutical production of protein therapeutics and vaccines. © 2010 Elsevier Inc. All rights reserved.


Receive press releases from iHealthcareAnalyst, Inc.: By Email Global Albumin Market USD 300 Million by 2020, Research Study Published by iHealthcareAnalyst, Inc. The global albumin market is estimated to reach USD 300 Million in 2020, expanding at a CAGR of 2.4% from 2016 to 2020. Maryland Heights, MO, November 01, 2016 --( Visit the Albumin Market 2013-2020 report at https://www.ihealthcareanalyst.com/report/albumin-market/ The global albumin market segmentation is based on type (human serum albumin, bovine serum albumin, recombinant albumin), and its applications (drug formulation and drug delivery, vaccines, components of media). The global albumin market report provides market size (Revenue USD Million 2013 to 2020), market share, market trends and forecasts growth trends (CAGR%, 2016 to 2020). Albumin is a concentrate of plasma proteins from blood and it works by increasing plasma volume or serum albumin levels. Albumin is used in treating a variety of conditions, including shock due to blood loss in the body, burns, low protein levels due to surgery or liver failure, and as an additional medicine in bypass surgery. The global albumin market research report is divided by geography (regional and country based) into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World. 1. Albumin Type 1.1 Human Serum Albumin(HSA) 1.2 Bovine Serum Albumin(BSA) 1.3 Recombinant Albumin(rAlbumin) 2. Application 2.1 Drug Formulation and Drug Delivery 2.2 Vaccines 2.3 Components of Media 3. Geography (Region, Country) 3.1 North America (U.S., Canada) 3.2 Latin America (Brazil, Mexico, Rest of LA) 3.3 Europe (U.K., Germany, France, Italy, Spain, Rest of EU) 3.4 Asia Pacific (Japan, China, India, Rest of APAC) 3.5 Rest of the World 4. Company Profiles 4.1 CSL Behring LLC 4.2 HiMedia Laboratories 4.3 InVitria (Ventria Bioscience) 4.4 MedxBio Pte.Ltd. 4.5 Mitsubishi Tanabe Pharma 4.6 Novozymes A/S 4.7 Octapharma AG 4.8 RayBiotech, Inc. 4.9 Sigma-Aldrich Corporation 4.10 Thermo Fisher Scientific, Inc. About Us iHealthcareAnalyst, Inc. is a global health care market research and consulting company providing market analysis, and competitive intelligence services to global clients. The Company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals. iHealthcareAnalyst, Inc. provides industry participants and stakeholders with strategically analyzed, unbiased view of market dynamics and business opportunities within its coverage areas. Contact Us iHealthcareAnalyst, Inc. 2109, Mckelvey Hill Drive, Maryland Heights, MO 63043 United States Email: sales@ihealthcareranalyst.com Website: https://www.ihealthcareanalyst.com Maryland Heights, MO, November 01, 2016 --( PR.com )-- According to a market research report Albumin Market 2013-2020, published by iHealthcareAnalyst, Inc., the global albumin market is estimated to reach USD 300 Million in 2020, expanding at a CAGR of 2.4% from 2016 to 2020.Visit the Albumin Market 2013-2020 report at https://www.ihealthcareanalyst.com/report/albumin-market/The global albumin market segmentation is based on type (human serum albumin, bovine serum albumin, recombinant albumin), and its applications (drug formulation and drug delivery, vaccines, components of media). The global albumin market report provides market size (Revenue USD Million 2013 to 2020), market share, market trends and forecasts growth trends (CAGR%, 2016 to 2020).Albumin is a concentrate of plasma proteins from blood and it works by increasing plasma volume or serum albumin levels. Albumin is used in treating a variety of conditions, including shock due to blood loss in the body, burns, low protein levels due to surgery or liver failure, and as an additional medicine in bypass surgery.The global albumin market research report is divided by geography (regional and country based) into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World.1. Albumin Type1.1 Human Serum Albumin(HSA)1.2 Bovine Serum Albumin(BSA)1.3 Recombinant Albumin(rAlbumin)2. Application2.1 Drug Formulation and Drug Delivery2.2 Vaccines2.3 Components of Media3. Geography (Region, Country)3.1 North America (U.S., Canada)3.2 Latin America (Brazil, Mexico, Rest of LA)3.3 Europe (U.K., Germany, France, Italy, Spain, Rest of EU)3.4 Asia Pacific (Japan, China, India, Rest of APAC)3.5 Rest of the World4. Company Profiles4.1 CSL Behring LLC4.2 HiMedia Laboratories4.3 InVitria (Ventria Bioscience)4.4 MedxBio Pte.Ltd.4.5 Mitsubishi Tanabe Pharma4.6 Novozymes A/S4.7 Octapharma AG4.8 RayBiotech, Inc.4.9 Sigma-Aldrich Corporation4.10 Thermo Fisher Scientific, Inc.About UsiHealthcareAnalyst, Inc. is a global health care market research and consulting company providing market analysis, and competitive intelligence services to global clients. The Company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals.iHealthcareAnalyst, Inc. provides industry participants and stakeholders with strategically analyzed, unbiased view of market dynamics and business opportunities within its coverage areas.Contact UsiHealthcareAnalyst, Inc.2109, Mckelvey Hill Drive,Maryland Heights, MO 63043United StatesEmail: sales@ihealthcareranalyst.comWebsite: https://www.ihealthcareanalyst.com Click here to view the list of recent Press Releases from iHealthcareAnalyst, Inc.


Steere A.N.,University of Vermont | Bobst C.E.,University of Massachusetts Amherst | Zhang D.,VENTRIA BIOSCIENCE | Pettit S.C.,InVitria | And 3 more authors.
Journal of Inorganic Biochemistry | Year: 2012

The Fe3+ binding protein human serum transferrin (hTF) is well known for its role in cellular iron delivery via the transferrin receptor (TFR). A new application is the use of hTF as a therapy and targeted drug delivery system for a number of diseases. Recently, production of hTF in plants has been reported; such systems provide a relatively inexpensive, animal-free (eliminating potential contamination by animal pathogens) method to produce large amounts of recombinant proteins for such biopharmaceutical applications. Specifically, the production of Optiferrin™ (hTF produced in rice, Oryza sativa, from InVitria) has been shown to yield large amounts of functional protein for use in culture medium for cellular iron delivery to promote growth. In the present work we describe further purification (by gel filtration) and characterization of hTF produced in rice (purified Optiferrin™) to determine its suitability in biopharmaceutical applications. The spectral, mass spectrometric, urea gel and kinetic analysis shows that purified Optiferrin™ is similar to recombinant nonglycosylated N-His tagged hTF expressed by baby hamster kidney cells and/or serum derived glycosylated hTF. Additionally, in a competitive immunoassay, iron-loaded Optiferrin™ is equivalent to iron-loaded N-His hTF in its ability to bind to the soluble portion of the TFR immobilized in an assay plate. As an essential requirement for any functional hTF, both lobes of purified Optiferrin™ bind Fe 3+ tightly yet reversibly. Although previously shown to be capable of delivering Fe3+ to cells, the kinetics of iron release from iron-loaded Optiferrin™/sTFR and iron-loaded N-His hTF/sTFR complexes differ somewhat. We conclude that the purified Optiferrin™ might be suitable for consideration in biopharmaceutical applications. © 2012 Elsevier Inc. All rights reserved.


Zhang D.,VENTRIA BIOSCIENCE | Lee H.-F.,University of Southern California | Pettit S.C.,InVitria | Zaro J.L.,University of Southern California | And 2 more authors.
BMC Biotechnology | Year: 2012

Background: Transferrin (TF) plays a critical physiological role in cellular iron delivery via the transferrin receptor (TFR)-mediated endocytosis pathway in nearly all eukaryotic organisms. Human serum TF (hTF) is extensively used as an iron-delivery vehicle in various mammalian cell cultures for production of therapeutic proteins, and is also being explored for use as a drug carrier to treat a number of diseases by employing its unique TFR-mediated endocytosis pathway. With the increasing concerns over the risk of transmission of infectious pathogenic agents of human plasma-derived TF, recombinant hTF is preferred to use for these applications. Here, we carry out comparative studies of the TFR binding, TFR-mediated endocytosis and cellular iron delivery of recombinant hTF from rice (rhTF), and evaluate its suitability for biopharmaceutical applications.Result: Through a TFR competition binding affinity assay with HeLa human cervic carcinoma cells (CCL-2) and Caco-2 human colon carcinoma cells (HTB-37), we show that rhTF competes similarly as hTF to bind TFR, and both the TFR binding capacity and dissociation constant of rhTF are comparable to that of hTF. The endocytosis assay confirms that rhTF behaves similarly as hTF in the slow accumulation in enterocyte-like Caco-2 cells and the rapid recycling pathway in HeLa cells. The pulse-chase assay of rhTF in Caco-2 and HeLa cells further illustrates that rice-derived rhTF possesses the similar endocytosis and intracellular processing compared to hTF. The cell culture assays show that rhTF is functionally similar to hTF in the delivery of iron to two diverse mammalian cell lines, HL-60 human promyelocytic leukemia cells (CCL-240) and murine hybridoma cells derived from a Sp2/0-Ag14 myeloma fusion partner (HB-72), for supporting their proliferation, differentiation, and physiological function of antibody production.Conclusion: The functional similarity between rice derived rhTF and native hTF in their cellular iron delivery, TFR binding, and TFR-mediated endocytosis and intracellular processing support that rice-derived rhTF can be used as a safe and animal-free alternative to serum hTF for bioprocessing and biopharmaceutical applications. © 2012 Zhang et al.; licensee BioMed Central Ltd.


Youngblood B.A.,Texas Tech University Health Sciences Center | Alfano R.,InVitria | Pettit S.C.,InVitria | Zhang D.,VENTRIA BIOSCIENCE | And 3 more authors.
Journal of Biotechnology | Year: 2014

Embryonic and induced pluripotent stem cells have the ability to differentiate into any somatic cell type, and thus have potential to treat a number of diseases that are currently incurable. Application of these cells for clinical or industrial uses would require an increase in production to yield adequate numbers of viable cells. However, the relatively high costs of cytokines and growth factors required for maintenance of stem cells in the undifferentiated state have the potential to limit translational research. Leukemia inhibitory factor (LIF), a member of the IL-6 cytokine family, is a key regulator in the maintenance of naïve states for both human and mouse stem cells. In this study, we describe a new recombinant human LIF (rhLIF) using a plant-based (rice) expression system. We found that rice-derived rhLIF possessed the same specific activity as commercial Escherichia coli-derived LIF and was capable of supporting mouse embryonic stem cell proliferation in the undifferentiated state as evidenced from pluripotency marker level analysis. Retention of the pluripotent state was found to be indistinguishable between rice-derived rhLIF and other recombinant LIF proteins currently on the market. © 2013 The Authors.


PubMed | Texas Tech University Health Sciences Center, InVitria and VENTRIA BIOSCIENCE
Type: | Journal: Journal of biotechnology | Year: 2014

Embryonic and induced pluripotent stem cells have the ability to differentiate into any somatic cell type, and thus have potential to treat a number of diseases that are currently incurable. Application of these cells for clinical or industrial uses would require an increase in production to yield adequate numbers of viable cells. However, the relatively high costs of cytokines and growth factors required for maintenance of stem cells in the undifferentiated state have the potential to limit translational research. Leukemia inhibitory factor (LIF), a member of the IL-6 cytokine family, is a key regulator in the maintenance of nave states for both human and mouse stem cells. In this study, we describe a new recombinant human LIF (rhLIF) using a plant-based (rice) expression system. We found that rice-derived rhLIF possessed the same specific activity as commercial Escherichia coli-derived LIF and was capable of supporting mouse embryonic stem cell proliferation in the undifferentiated state as evidenced from pluripotency marker level analysis. Retention of the pluripotent state was found to be indistinguishable between rice-derived rhLIF and other recombinant LIF proteins currently on the market.

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