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CartSwine IL-3 (Yeast-derived Recombinant Protein) - 100 micrograms
Bulk quantities of Swine IL-3 protein are available.
Please contact us for pricing.
Swine IL-3 Specifications
Molecular Weight (calculated) - 13.7kDa
Amino Acid Sequence - MPTTTLQPKN YLAMIQEITR SLENLTVTSN KSLTLNELET LVNNTLLRPN LEAFVTFAEN HLKNISGIKK NLEKFRPILP TSMSTEEPIS IEEGDLGDFR AKLMEYLVVL RDSLKPMITE P (121)
Gene ID - Sequence based on published sequence. Hermanrud CE, et al., Expression and purification of non-N-glycosylated porcine interleukin 3 in yeast Pichia pastoris. Protein Expr Purif. 2012 Mar;82(1):70-4. doi: 10.1016/j.pep.2011.11.011. Epub 2011 Dec 1.
Homology Across Species
Sus scrofa (pig) IL-3 - 100%
More - https://blast.ncbi.nlm.nih.gov/
Endotoxin - Naturally endotoxin-free
Applications
Cell Culture, ELISA Standard, Western Blot Control
IL-3 Background
IL-3 (Interleukin-3) stimulates the differentiation of multipotent hematopoietic stem cells into myeloid progenitor cells or, with the addition of IL-7, into lymphoid progenitor cells. IL-3 also stimulates proliferation of all cells in the myeloid lineage (granulocytes, monocytes, and dendritic cells), in conjunction with other cytokines, e.g., Erythropoietin (EPO), Granulocyte macrophage colony-stimulating factor (GM-CSF), and IL-6. It is secreted by basophils and activated T cells to support growth and differentiation of T cells from the bone marrow in an immune response.
Alternate Names - IL3, interleukin 3, IL-3, MCGF, MULTI-CSF
MPTTTLQPKN YLAMIQEITR SLENLTVTSN KSLTLNELET LVNNTLLRPN LEAFVTFAEN HLKNISGIKK NLEKFRPILP TSMSTEEPIS IEEGDLGDFR AKLMEYLVVL RDSLKPMITE P (121)
Sequence based on published sequence. Hermanrud CE, et al., Expression and purification of non-N-glycosylated porcine interleukin 3 in yeast Pichia pastoris. Protein Expr Purif. 2012 Mar;82(1):70-4. doi: 10.1016/j.pep.2011.11.011. Epub 2011 Dec 1.
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.
Abstract
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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