List of recombinant proteins: Difference between revisions
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* [[Follicle-stimulating hormone]] (FSH) as a recombinant [[gonadotropin preparation]] replaced Serono's [[Pergonal]] which was previously isolated from post-menopausal female urine |
* [[Follicle-stimulating hormone]] (FSH) as a recombinant [[gonadotropin preparation]] replaced Serono's [[Pergonal]] which was previously isolated from post-menopausal female urine |
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* [[Factor VIII]]: [[Kogenate]] from [[Bayer]] replaced [[blood]] harvested factor VIII |
* [[Factor VIII]]: [[Kogenate]] from [[Bayer]] replaced [[blood]] harvested factor VIII |
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* [[Ribosomal proteins]]: For the studies of individual ribosomal proteins, the use of proteins that are produced and purified from recombinant sources<ref>{{cite journal|author=Danilo Correddu, José de Jesús Montaño López, Praveen G. Vadakkedath, Amy Lai, Jane I. Pernes, Paris R. Watson, Ivanhoe K. H. Leung |journal= [[Scientific Reports | Sci. Rep.]]|title=An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli.|volume=9|pages=8884|PMC=|PMID=|date=2019|language=English|doi=10.1038/s41598-019-45323-8}}</ref><ref>{{cite journal|author=N. M. Parakhnevitch, A. A. Malygin, G. G. Karpova |journal= [[Biokhimiya | Biochemistry (Moscow)]]|title=Recombinant human ribosomal protein S16: expression, purification, refolding, and structural stability.|volume=70|pages=777-781|PMC=|PMID=16097941|date=2005|language=English|doi=10.1007/s10541-005-0183-3}}</ref><ref>{{cite journal|author=Alexey Malygin, Oxana Baranovskaya, Anton Ivanov, Galina Karpova |journal= [[Protein_Expression_and_Purification_(journal) | Protein Expr. Purif.]]|title=Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26.|volume=28|pages=57–62|PMC=|PMID=12651107|date=2003|language=English|doi=10.1016/S1046-5928(02)00652-6}}</ref><ref>{{cite journal|author=Marek Tchórzewski, Aleksandra Boguszewska, Dariusz Abramczyk, Nikodem Grankowski |journal= [[Protein_Expression_and_Purification_(journal) | Protein Expr. Purif.]]|title=Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae.|volume=15|pages=40–47|PMC=|PMID=10024468|date=1999|language=English|doi=10.1006/prep.1998.0997}}</ref> has largely replaced those that are obtained through isolation.<ref>{{cite journal|author=E Collatz, N Ulbrich, K Tsurugi, H N Lightfoot, W MacKinlay, A Lin and I G Wool |journal= [[Journal_of_Biological_Chemistry | J. Biol. Chem.]]|title=Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26, S27', and 29. |volume=252 |pages=9071-9080 |PMC=|PMID=925037 |date=1977|language=English|doi=}}</ref><ref>{{cite journal|author=Samuel Fogel, Paul S. Sypherd |journal= [[Journal_of_Bacteriology | J. Bacteriol. ]]|title=Extraction and Isolation of Individual Ribosomal Proteins from Escherichia coli. |volume=96 |pages=358–364 |PMC=252306 |PMID=4877123 |date=1968|language=English|doi=}}</ref> However, isolation is still required for the studies of the whole [[ribosome]].<ref>{{cite journal|author=Preeti Mehta, Perry Woo, Krithika Venkataraman, A. Wali Karzai |journal= [[Methods_in_Molecular_Biology | Methods Mol. Biol. ]]|title=Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome. |volume=905 |pages=273–289 |PMC=4607317 |PMID=22736011 |date=2012 |language=English |doi= 10.1007/978-1-61779-949-5_18}}</ref><ref>{{cite journal|author=Stéphane Belin, Sabine Hacot, Lionel Daudignon, Gabriel Therizols, Stéphane Pourpe, Hichem C. Mertani, Manuel Rosa‐Calatrava, Jean‐Jacques Diaz |journal= [[Current Protocols | Curr. Protoc. Cell Biol. ]]|title=Purification of ribosomes from human cell lines. |volume=49 |pages=3.40.1-3.40.11 |PMC= |PMID=21154551 |date=2010 |language=English |doi= 10.1002/0471143030.cb0340s49}}</ref> |
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==Human recombinants with recombination as only source== |
==Human recombinants with recombination as only source== |
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Revision as of 01:07, 21 June 2019
The following is a list of notable proteins that are generated from recombinant DNA, using biomolecular engineering, focusing on those that are used in human and veterinary medicine. In many cases, recombinant human proteins have replaced the original animal-derived version used in medicine. The prefix "rh" for "recombinant human" appears less and less in the literature.
A much larger number of recombinant proteins is used in the research laboratory. These include both commercially available proteins (for example most of the enzymes used in the molecular biology laboratory), and those that are generated in the course specific research projects.
Human recombinants that largely replaced animal or harvested from human types
- Human growth hormone (rHGH): Humatrope from Lilly and Serostim from Serono replaced cadaver harvested human growth hormone
- human insulin (BHI): Humulin from Lilly and Novolin from Novo Nordisk among others largely replaced bovine and porcine insulin for human therapy. Some prefer to continue using the animal-sourced preparations, as there is some evidence that synthetic insulin varieties are more likely to induce hypoglycemia unawareness. Remaining manufacturers of highly purified animal-sourced insulin include the U.K.'s Wockhardt Ltd. (headquartered in India), Argentina's Laboratorios Beta S.A., and China's Wanbang Biopharma Co.
- Follicle-stimulating hormone (FSH) as a recombinant gonadotropin preparation replaced Serono's Pergonal which was previously isolated from post-menopausal female urine
- Factor VIII: Kogenate from Bayer replaced blood harvested factor VIII
- Ribosomal proteins: For the studies of individual ribosomal proteins, the use of proteins that are produced and purified from recombinant sources[1][2][3][4] has largely replaced those that are obtained through isolation.[5][6] However, isolation is still required for the studies of the whole ribosome.[7][8]
Human recombinants with recombination as only source
- Erythropoietin (EPO): Epogen from Amgen
- Granulocyte colony-stimulating factor (G-CSF): filgrastim sold as Neupogen from Amgen; pegfilgrastim sold as Neulasta
- alpha-galactosidase A: Fabrazyme by Genzyme
- alpha-L-iduronidase: (rhIDU; laronidase) Aldurazyme by BioMarin Pharmaceutical and Genzyme
- N-acetylgalactosamine-4-sulfatase (rhASB; galsulfase): Naglazyme by BioMarin Pharmaceutical
- Dornase alfa, a DNase sold under the trade name Pulmozyme by Genentech
- Tissue plasminogen activator (TPA) Activase by Genentech
- Glucocerebrosidase: Ceredase by Genzyme
- Interferon (IF) Interferon-beta-1a: Avonex from Biogen Idec; Rebif from Serono; Interferon beta-1b as Betaseron from Schering
- Insulin-like growth factor 1 (IGF-1)
- Rasburicase, a Urate Oxidase analog sold as Elitek from Sanofi
Animal recombinants
- Bovine somatotropin (bST)
- Porcine somatotropin (pST)
- Bovine Chymosin
Viral recombinants
- Envelope protein of the hepatitis B virus marketed as Engerix-B by SmithKline Beecham
- HPV Vaccine proteins
External links
- ^ Danilo Correddu, José de Jesús Montaño López, Praveen G. Vadakkedath, Amy Lai, Jane I. Pernes, Paris R. Watson, Ivanhoe K. H. Leung (2019). "An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli". Sci. Rep. 9: 8884. doi:10.1038/s41598-019-45323-8.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ N. M. Parakhnevitch, A. A. Malygin, G. G. Karpova (2005). "Recombinant human ribosomal protein S16: expression, purification, refolding, and structural stability". Biochemistry (Moscow). 70: 777–781. doi:10.1007/s10541-005-0183-3. PMID 16097941.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Alexey Malygin, Oxana Baranovskaya, Anton Ivanov, Galina Karpova (2003). "Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26". Protein Expr. Purif. 28: 57–62. doi:10.1016/S1046-5928(02)00652-6. PMID 12651107.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Marek Tchórzewski, Aleksandra Boguszewska, Dariusz Abramczyk, Nikodem Grankowski (1999). "Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae". Protein Expr. Purif. 15: 40–47. doi:10.1006/prep.1998.0997. PMID 10024468.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ E Collatz, N Ulbrich, K Tsurugi, H N Lightfoot, W MacKinlay, A Lin and I G Wool (1977). "Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26, S27', and 29". J. Biol. Chem. 252: 9071–9080. PMID 925037.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Samuel Fogel, Paul S. Sypherd (1968). "Extraction and Isolation of Individual Ribosomal Proteins from Escherichia coli". J. Bacteriol. . 96: 358–364. PMC 252306. PMID 4877123.
- ^ Preeti Mehta, Perry Woo, Krithika Venkataraman, A. Wali Karzai (2012). "Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome". Methods Mol. Biol. . 905: 273–289. doi:10.1007/978-1-61779-949-5_18. PMC 4607317. PMID 22736011.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Stéphane Belin, Sabine Hacot, Lionel Daudignon, Gabriel Therizols, Stéphane Pourpe, Hichem C. Mertani, Manuel Rosa‐Calatrava, Jean‐Jacques Diaz (2010). "Purification of ribosomes from human cell lines". Curr. Protoc. Cell Biol. . 49: 3.40.1-3.40.11. doi:10.1002/0471143030.cb0340s49. PMID 21154551.
{{cite journal}}: CS1 maint: multiple names: authors list (link)