Recombinant MPL Protein from antibodies-online

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Recombinant MPL Protein

Description

Product Characteristics: Made in Germany - from design to production - by highly experienced protein experts. Human MPL Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade. State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a made to order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization).

When you order this made-to-order protein you will only pay upon receival of the correctly folded protein. With no financial risk on your end you can rest assured that our experienced protein experts will do everything to make sure that you receive the protein you ordered.

The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.
antibodies-online can provide customization with regards to expression system, tag location and sequence for our made to order proteins designed and produced in Germany. Please contact our customer support for further information.:

Target Information: 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]