Rat Mpl (His) Insect Cell Lysate

Name: Rat Mpl (His) Insect Cell Lysate
SKU: CLOE-1956
Availability: InStock

For research use only. Not intended for any clinical use.

Cat. No. : CLOE-1956 Host Cell : Baculovirus-Insect cell

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Cell Lysate Information

Gene Information

Cat. No.	CLOE-1956
Description	This cell lysate overexpresses the mature form of rat Mpl (Met1-Ala500) with a C-terminal polyhistidine tag. Purification of target protein from this cell lysate has been verified.
Introduction	This cell lysate overexpresses the mature form of rat Mpl (Met1-Ala500) with a C-terminal polyhistidine tag. Purification of target protein from this cell lysate has been verified.
Target Gene	Mpl
Host Cell	Baculovirus-Insect cell
Applications	Positive control for Western Blot (WB), antibody verification, protein purification.
Storage	Upon receipt, store at 4℃ , or prepare aliquots and store at -80℃. Multiple freeze-thaw cycles should be avoided.
Shipping	Ice package

Target Gene

MPL

Background

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]

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