Recombinant Human EPO Protein, >95% (SDS-PAGE and HPLC), high purity

Features and benefits
  • Expression System: CHO
  • Accession #: P01588
  • Protein Tag: C-Fc
  • Bioactivity: Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. The ED50 for this effect is typically less than 5.0 ng/mL.
  • Endotoxin Concentration: <20 EU/mg
Item Number
rp145653
Grouped product items
SKUSizeAvailabilityPrice Qty
rp145653-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$89.90
rp145653-50μg
50μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$259.90
rp145653-100μg
100μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$399.90
rp145653-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$1,499.90

GMP, >95% (SDS-PAGE and HPLC), Active, CHO, Fc tag, 28-193 aa

Basic Description

Product NameRecombinant Human EPO Protein, >95% (SDS-PAGE and HPLC), high purity
SynonymsEP; EPO; EPO alpha; Epoetin; Erythropoetin; Erythropoietin precursor; MVCD2; RhEPO
GradeActiBioPure™, Azide Free, Bioactive, Carrier Free, GMP, High Performance
Product Description

Purity

≥ 95% SDS-PAGE; HPLC


Relevance

Human erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals.


Specifications & PurityActiBioPure™, Bioactive, GMP, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE&HPLC)
Purity>95% (SDS-PAGE and HPLC)
BioactivityMeasured in a cell proliferation assay using TF‑1 human erythroleukemic cells. The ED50 for this effect is typically less than 5.0 ng/mL.
Endotoxin Concentration<20 EU/mg
Expression SystemCHO
SpeciesHuman
Amino Acids28-193 aa
SequenceAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
Protein TagC-Fc
Accession #P01588
Predicted molecular weight58 kDa
SDS-PAGE61.8 kDa, under reducing conditions.

Images

Recombinant Human EPO Protein (rp145653) - Protein Bioactivity
Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. The ED₅₀ for this effect is typically less than 5.0 ng/mL.

Recombinant Human EPO Protein (rp145653) - SDS-PAGE
2.5 μg/lane of Recombinant Human EPO was resolved with SDS-PAGE under reducing (R) and visualized by Coomassie® Blue staining, showing a band at 61.8 kDa.

Product Specifications

FormLyophilized
ReconstitutionWe recommend that this vial be briefly centrifuged prior to opening to bring the contents to thebottom. Reconstitute in sterile water for injection to a concentration of 100μg/mL. Stock solutions should be apportioned into working aliquots and stored at
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageUpon delivery aliquot, Store at -20°C, Avoid freeze / thaw cycles. Lyophilized with no additives. This product is an active protein and may elicit a biological response in vivo, handle with caution.

Certificates

Certificate of Analysis(COA)

Enter Lot Number to search for COA:

Find and download the COA for your product by matching the lot number on the packaging.

3 results found

Lot NumberCertificate TypeDateItem
ZJ23F1001348Certificate of AnalysisOct 19, 2023 rp145653
ZJ23F1001349Certificate of AnalysisOct 19, 2023 rp145653
ZJ23F1001350Certificate of AnalysisOct 19, 2023 rp145653

Related Documents

References

1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P et al..  (2004)  The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)..  Genome Res,  14  (10B): (2121-7).  [PMID:15489334]
2. Syed RS, Reid SW, Li C, Cheetham JC, Aoki KH, Liu B, Zhan H, Osslund TD, Chirino AJ, Zhang J et al..  (1998)  Efficiency of signalling through cytokine receptors depends critically on receptor orientation..  Nature,  395  (6701): (511-6).  [PMID:9774108]
3. Takeuchi, M M and Kobata, A A..  (1991)  Structures and functional roles of the sugar chains of human erythropoietins..  Glycobiology,      [PMID:1820196]
4. Sasaki, H H, Ochi, N N, Dell, A A and Fukuda, M M..  (1988)  Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometry..  Biochemistry,    (15):   [PMID:3219367]
5. Takeuchi, M M and 6 more authors..  (1988)  Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells..  The Journal of biological chemistry,    (15):   [PMID:3346214]
6. Jacobs, K K and 9 more authors..  (1985)  Isolation and characterization of genomic and cDNA clones of human erythropoietin..  Nature,      [PMID:3838366]
7. Lin, F K FK and 9 more authors..  (1985)  Cloning and expression of the human erythropoietin gene..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:3865178]
8. Lai, P H PH, Everett, R R, Wang, F F FF, Arakawa, T T and Goldwasser, E E..  (1986)  Structural characterization of human erythropoietin..  The Journal of biological chemistry,    (5):   [PMID:3949763]
9. Yanagawa, S S and 6 more authors..  (1984)  Isolation of human erythropoietin with monoclonal antibodies..  The Journal of biological chemistry,    (10):   [PMID:6698989]
10. Funakoshi, A A, Muta, H H, Baba, T T and Shimizu, S S..  (1993)  Gene expression of mutant erythropoietin in hepatocellular carcinoma..  Biochemical and biophysical research communications,    (15):   [PMID:8396923]
11. Glöckner, G G and 6 more authors..  (1998)  Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes..  Genome research,      [PMID:9799793]
12. Hillier, Ladeana W LW and 106 more authors..  (2003)  The DNA sequence of human chromosome 7..  Nature,    (10):   [PMID:12853948]
13. Tong, Zongzhong Z and 36 more authors..  (2008)  Promoter polymorphism of the erythropoietin gene in severe diabetic eye and kidney complications..  Proceedings of the National Academy of Sciences of the United States of America,    (13):   [PMID:18458324]
14. Camps, Carme C and 10 more authors..  (2016)  Gene panel sequencing improves the diagnostic work-up of patients with idiopathic erythrocytosis and identifies new mutations..  Haematologica,      [PMID:27651169]
15. Kim, Ah Ram AR and 20 more authors..  (2017)  Functional Selectivity in Cytokine Signaling Revealed Through a Pathogenic EPO Mutation..  Cell,    (9):   [PMID:28283061]
16. Zmajkovic, Jakub J and 6 more authors..  (2018)  A Gain-of-Function Mutation in EPO in Familial Erythrocytosis..  The New England journal of medicine,    (8):   [PMID:29514032]

Solution Calculators