重组人血小板生成素受体蛋白/Recombinant human TPOR protein, N-His说明书-分析方法-资讯-生物在线

重组人血小板生成素受体蛋白/Recombinant human TPOR protein, N-His说明书

作者:上海钰博生物科技有限公司 2023-03-29T00:00 (访问量:189)

 Recombinant human TPOR protein, N-His

重组人血小板生成素受体蛋白

英文名称 Recombinant human TPOR protein, N-His
中文名称 重组人血小板生成素受体蛋白
别    名 C MPL; C-MPL; CMPL; CD110; CD 110; MPL; MPLV; Myeloproliferative leukemia protein; Myeloproliferative leukemia virus oncogene; Proto-oncogene c-Mpl; THCYT2; Thrombopoietin receptor; TPO R; TPO-R; TPOR_HUMAN.  
理论分子量 27.4kDa
性    状 Lyophilized or Liquid
浓    度 >1mg/ml
物    种 Human
序    列 297-482/635
纯    度 >90% as determined by SDS-PAGE
纯化方法 AC
内毒素 Not analyzed
表达系统 E.coli
活性 Not tested
标签 N-His
缓 冲 液 4M Urea
保存条件 Stored at -70℃ or -20℃. Avoid repeated freeze/thaw cycles.
注意事项 This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
产品介绍 In 1990 an oncogene, v-mpl, was identified from the murine myeloproliferative leukemia virus that was capable of immortalizing bone marrow hematopoietic cells from different lineages. In 1992 the human homologue, named, c-mpl, was cloned. Sequence data revealed that c-mpl encoded a protein that was homologous with members of the hematopoietic receptor superfamily. Presence of anti-sense oligodeoxynucleotides of c-mpl inhibited megakaryocyte colony formation. The ligand for c-mpl, thrombopoietin, was cloned in 1994. Thrombopoietin was shown to be the major regulator of megakaryocytopoiesis and platelet formation. The protein encoded by the c-mpl gene, CD110, is a 635 amino acid transmembrane domain, with two extracellular cytokine receptor domains and two intracellular cytokine receptor box motifs . TPO-R deficient mice were severely thrombocytopenic, emphasizing the important role of CD110 and thrombopoietin in megakaryocyte and platelet formation. Upon binding of thrombopoietin CD110 is dimerized and the JAK family of non-receptor tyrosine kinases, as well as the STAT family, the MAPK family, the adaptor protein Shc and the receptors themselves become tyrosine phosphorylated. [provided by RefSeq, Jul 2008]
 
产品图片
The purity of the protein is greater than 90% as determined by reducing SDS-PAGE.

本产品仅供科研使用.请勿用于医药,不能用于临床治疗诊断使用!

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