erythropoietin   Click here for help

GtoPdb Ligand ID: 4921

Synonyms: Epogen® | Procrit®
Approved drug
erythropoietin is an approved drug (FDA (no history prior to 1989 available))
Compound class: Endogenous peptide in human, mouse or rat
Comment: Recombinant forms of human erythropoietin (epoetins), are contained in various approved drugs with INNs that reflect the different glycoform structures formed by different manufacturing processes. The table below provides details of the epoetin alpha originator drug and biosimilars that are currently approved for use by the US FDA and/or the European Medicines Agency (EMA).

Epoetin alpha and biosimilar drugs.

INNTrade names (authorisation holder)First FDA approvalFirst EMA approval
epoetin alfaBinocrit (Sandoz), Abseamed (Medice Arzneimittel Pütter), Epogen (Amgen), Procrit (Janssen)19892007
epoetin betaNeoRecormon, Recormon (both Roche)n/a1997
epoetin zeta (a.k.a. epoetin alfa-epbx)Silapo (Stada Arzneimitte), Retacrit (Hospira)20182007
epoetin thetaBiopoin (Teva), Eporatio (Ratiopharm)n/a2009
Species: Human
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Ligand Activity Visualisation Charts

These are box plot that provide a unique visualisation, summarising all the activity data for a ligand taken from ChEMBL and GtoPdb across multiple targets and species. Click on a plot to see the median, interquartile range, low and high data points. A value of zero indicates that no data are available. A separate chart is created for each target, and where possible the algorithm tries to merge ChEMBL and GtoPdb targets by matching them on name and UniProt accession, for each available species. However, please note that inconsistency in naming of targets may lead to data for the same target being reported across multiple charts.

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View interactive charts of activity data across species

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View more information in the IUPHAR Pharmacology Education Project: erythropoietin

Peptide Sequence Click here for help
APPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQAL
LVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEA
CRTGDR
Selected 3D Structures
PDB Id: 1BUY
Image of ligand 3D structure from RCSB PDB
Post-translational Modification
N-linked glycosylation of asparagine residues at positions 24, 38, and 83; O-linked glycosylation of serine at position 126; disulphide bond formation between cysteine residues at positions 7 and 161, and 29 and 33