Are you working with human, mouse or monkey models in your EPO research? We can provide the tools to you.



Analyse isoforms

Purification of EPO removes the major proportion of other proteins and can also concentrate your sample. Our purification tools can be used to purify EPO from different biological fluids, including DBS samples, as well as from cell culture media.

Quantification of the total amount of EPO can be done in some biological fluids directly or after purification. Our EPO Semi Quantification kit is in easy-to-use dipstick format.

Posttranslational modifications of a protein, such as glycosylation, can significantly impact its biological functions. Differences in the EPO isoform pattern may occur between EPO produced in different cell types, such as liver or kidney cells, between normal cells and tumour cells, or between human cells and cells from other species, such as many recombinant EPO variants.

Our isoform test is built on a dipstick, combining affinity chromatography and EPO immuno assay.

Research articles from some of our customers:

“A simple method to immunopurify erthyropoiesis stimulating agents from urine, aiming to optimize erythropoietin screening by SAR‐PAGE“

Author(s): Heiland C, et al.

“Increased Synthesis of Liver Erythropoietin with CKD”

Author(s): de Seigneux S, et al.

“Fc-fragment removal allows the EPO-Fc fusion protein to be detected in blood samples by IEF-PAGE”

Author(s): Postnikov P, et al.

“Recombinant erythropoietin in humans has a prolonged effect on circulating erythropoietin isoform distribution”

Author(s): Aachmann-Andersen N.J, et al.

“Kidney-synthesized erythropoietin is the main source for the hypoxia-induced increase in plasma erythropoietin in adult humans”

Author(s): Lundby AK, et al.

“Detection of microdoses of rhEPO with the MAIIA test”

Author(s): J. Mørkeberg K, et al.

“A new analytical method based on anti-EPO monolith column and LC-FAIMS-MS/MS for the detection of rHuEPOs in horse plasma and urine samples”

Author(s): Ludovic Bailly-Chouriberry, et al.
doi:10.1039/C2AN15662H     Analyst. 137(10), 2445-2453 (2012).

“Detection of recombinant human EPO administered to horses using MAIIA lateral flow isoform test”

Author(s): Lönnberg M, et al.
doi:10.1007/s00216-012-5972-0 Anal. Bioanal. Chem. 403(6), 1619-1628 (2012).

“Rapid detection of erythropoiesis-stimulating agents in urine and serum”

Author(s): Lönnberg M, et al.
doi:10.1016/j.ab.2011.09.021  Anal. Biochem. 420(2), 101-114 (2012).

“Erythropoietin (EPO) immunoaffinity columns–a powerful tool for purifying EPO and its recombinant analogues”

Author(s): Dehnes Y, et al.
doi:10.1016/j.jpba.2010.06.017 J. Pharm. Biomed. Anal. 53(4), 1028-1032 (2010).

“Rapid affinity purification of erythropoietin from biological samples using disposable monoliths”

Author(s): Lönnberg M, et al.
doi:10.1016/j.chroma.2010.09.034 J. Chromatogr. A 1217, 7031-7037 (2010).

“Ultra-sensitive immunochromatographic assay for quantitative determination of erythropoietin”

Author(s): Lönnberg M, et al.
doi:10.1016/j.jim.2008.09.022 J. Immunol. Meth. 339, 236-244 (2008).

“Lectin affinity chromatography as a tool to differentiate endogenous and recombinant erythropoietins”

Author(s): L Franco Fraguas, et al.
doi:10.1016/j.chroma.2008.10.036 J. Chromatogr. A 1212, 82-88 (2008).


“Membrane-Assisted Isoform ImmunoAssay: Separation and determination of protein isoforms”

Author(s): Lönnberg M
Doctoral thesis, ISBN: 91-554-5250-7, Uppsala University, Sweden (2002).

“Chromatographic performance of a thin microporous bed of nitrocellulose”

Author(s): Lönnberg M, et al.
doi:10.1016/S0378-4347(01)00376-0 J. Chrom. B 763, 107-120 (2001).

“Membrane assisted isoform immunoassay: a rapid method for the separation and determination of protein isoforms in an integrated immunoassay”

Author(s): Lönnberg M, et al.
doi:10.1016/S0022-1759(00)00287-8 J. Immunol. Meth. 246, 25-36 (2000).

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