Bulk quantities of Swine EPO protein are available.
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Molecular Weight (calculated) - 18.6kDa
Amino Acid Sequence - APPRLICDSR VLERYILEAK EGENATMGCA ESCSFSENIT VPDTKVNFYA WKRMEVQQQA MEVWQGLALL SEAILQGQAL LANSSQPSEA LQLHVDKAVS GLRSLTSLLR ALGAQKEAIP LPDASPSSAT PLRTFAVDTL CKLFRNYSNF LRGKLTLYTG EACRRRDR (168)
Gene ID - 397249
Homology Across Species
Sus scrofa (pig) EPO – 100%
More - https://blast.ncbi.nlm.nih.gov/
Endotoxin - Naturally endotoxin-free
Cell Culture, ELISA Standard, Western Blot Control
Erythropoietin (EPO) is an essential hormone for red blood cell production. Without it, definitive erythropoiesis does not take place. Erythropoietin has its primary effect on red blood cell progenitors and precursors by promoting their survival through protecting these cells from apoptosis. It is the primary erythropoietic factor that cooperates with various other growth factors (e.g., IL-3, IL-6, glucocorticoids, and SCF) involved in the development of erythroid lineage from multipotent progenitors. Erythropoietin has a range of actions including vasoconstriction-dependent hypertension, stimulating angiogenesis, and inducing proliferation of smooth muscle fibers. It can increase iron absorption by suppressing the hormone hepcidin. EPO is highly glycosylated, with half-life in blood around five hours. The half-life of EPO may vary between endogenous and various recombinant versions. Additional glycosylation or other alterations of EPO via recombinant technology have led to increased stability in blood. EPO binds to the erythropoietin receptor on the red cell progenitor surface and activates a JAK2 signaling cascade. Erythropoietin receptor expression is found in a number of tissues, such as bone marrow and peripheral/central nervous tissue. In the bloodstream, red cells themselves do not express erythropoietin receptor, so cannot respond to EPO. However, indirect dependence of red cell longevity in the blood on plasma erythropoietin levels has been reported, a process termed neocytolysis.
Alternate Names - EPO, EP, MVCD2, erythropoietin, Erythropoietin, ECYT5, DBAL
Generation of human endothelium in pig embryos deficient in ETV2.
Das S, Koyano-Nakagawa N, Gafni O, Maeng G, Singh BN, Rasmussen T, Pan X, Choi KD, Mickelson D, Gong W, Pota P, Weaver CV, Kren S, Hanna JH, Yannopoulos D, Garry MG, Garry DJ.
Nat Biotechnol. 2020 Mar;38(3):297-302. doi: 10.1038/s41587-019-0373-y. Epub 2020 Feb 24.
Applications: The proteins were used in a hematopoietic assay which used cells from embryoid bodies.
The scarcity of donor organs may be addressed in the future by using pigs to grow humanized organs with lower potential for immunological rejection after transplantation in humans. Previous studies have demonstrated that interspecies complementation of rodent blastocysts lacking a developmental regulatory gene can generate xenogeneic pancreas and kidney1,2. However, such organs contain host endothelium, a source of immune rejection. We used gene editing and somatic cell nuclear transfer to engineer porcine embryos deficient in ETV2, a master regulator of hematoendothelial lineages3-7. ETV2-null pig embryos lacked hematoendothelial lineages and were embryonic lethal. Blastocyst complementation with wild-type porcine blastomeres generated viable chimeric embryos whose hematoendothelial cells were entirely donor-derived. ETV2-null blastocysts were injected with human induced pluripotent stem cells (hiPSCs) or hiPSCs overexpressing the antiapoptotic factor BCL2, transferred to synchronized gilts and analyzed between embryonic day 17 and embryonic day 18. In these embryos, all endothelial cells were of human origin.
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