EPO, Human

ArtNr	Z02975-50
Hersteller	GenScript
Menge	50 ug
Quantity options	1 mg 10 ug 50 ug
Kategorie	Neuroscience Molecular Targets for Neuroscience Targets for Rodent Neurosciences Peptides & Proteins Recombinant Proteins Cell Biology Cell Culture Cytokines Cardiovascular Research Hypertension
Typ	Proteins
Specific against	Human (Homo sapiens)
Purity	> 95% as analyzed by SDS-PAGE and HPLC.
Sequence	Ala28-Arg193(Accession # CAA26094)
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	protein/Z02975_50-Erythropoietin_EPO_Human,Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients. The cDNAs for EPO have been cloned from human, mouse, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.</td></tr><tr><th>M.W.</th><td colspan="7"> Mature human EPO, containing 166 amino acid residues, has a predicted molecular mass of approximately 21 kDa. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 26-36 kDa in SDS-PAGE.</td></tr><tr><th>Purity</th><td colspan="7"> > 95% as analyzed by SDS-PAGE and HPLC.</td></tr><tr><th>Endotoxin Level</th><td colspan="7"> <0.2 EU/ug, determined by LAL method.</td></tr><tr><th>Specific Activity</th><td colspan="7"> ED50 1 x 106units/mg</td></tr><tr><th>Storage</th><td colspan="7"> Lyophilized recombinant, human EPO, remains stable up to 6 months at -80C from date of receipt. Upon reconstitution, rhEPO should be stable up to 1 week at 4C or up to 2 months at -20C.</td></tr><tr><th>Formulation</th><td colspan="7"> Lyophilized after extensive dialysis against PBS.</td></tr><tr><th>Reconstitution</th><td colspan="7"> Reconstituted in ddH2O or PBS at 100 ug/ml.</td></tr><tr><th>Sequence</th><td colspan="7"> Ala28-Arg193(Accession
Similar products	Erythropoietin
Versandbedingung	Gekühlt
Lieferbar
Specificity	ED50 1 x 106units/mg
Manufacturer - Category	Proteins
Country of Origin	USA
Shipping Temperature	4°C
Storage Conditions	-80°C
Molecular Weight	Mature human EPO, containing 166 amino acid residues, has a predicted molecular mass of approximately 21 kDa. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 26-36 kDa in SDS-PAGE.
Product Line	Cytokines
Manufacturer - Specificity	ED50 1 x 106units/mg
Description	Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients. The cDNAs for EPO have been cloned from human, mouse, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.
Reconstitution	Reconstituted in ddH2O or PBS at 100 ug/ml.
Formulation	Lyophilized after extensive dialysis against PBS.
Endotoxin Level	<0.2 EU/ug, determined by LAL method.
Notes	For research use only

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