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MTOR/RAPTOR/MLST8 HUMAN
Кат. №: SRP0364-10UG
Производитель: Sigma-Aldrich
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MTOR/RAPTOR/MLST8 HUMAN
Кат. №: SRP0364-10UG
Производитель: Sigma-Aldrich
Кол-во:
Цена по запросу
Товар оформляется под заказ
Кол-во:
Цена по запросу
Товар оформляется под заказ
Description_x000D_
General description_x000D_
This product (recombinant mTOR/Raptor/MLST8) is a complex of human mechanistic target of rapamycin (mTOR), also known as FRAP1 (GenBank Accession No. NM_004958), amino acids 1362-end with N-terminal FLAG-tag, MW = 137 kDa; human MTOR associated protein, LST8 homolog (MLST8) (GenBank Accession No. NM_022372) amino acids 2-326 (end) with N-terminal His-tag, MW = 37 kDa and human regulatory associated protein of MTOR complex 1 (Raptor) (GenBank Accession No. NM_020761) amino acids 2-1335 (end) with N-terminal His-tag, MW=150 kDa, co-expressed in a Baculovirus-infected Sf9 cell expression system._x000D_
Application_x000D_
Recombinant mTOR/Raptor/MLST8 has been used in in vitro caspase reactions._x000D_
Biochem/physiol Actions_x000D_
Mechanistic target of rapamycin (mTOR) modulates cell growth and division by integrating nutrient and mitogen signals. It also modulates the functions of antigen-presenting cells, like dendritic cells and activates T-cells. mTOR is also involved in innate and adaptive immunity. MTOR associated protein, LST8 homolog (MLST8) is a subunit of both the mTOR complex 1 and 2 (mTORC1 and 2). It is crucial for the activation of the mTOR kinase and is a regulator of mTOR pathways. Regulatory associated protein of MTOR complex 1 (RAPTOR) has an important role in modulating cell growth and in energy homeostasis as a scaffolding protein. It takes part in recruiting substrates of mechanistic target of rapamycin (mTOR) to the rapamycin-sensitive mTOR complex 1 (mTORC1). RAPTOR also associates with proteins involved in the pathway and aids in phosphorylating them.
Related Categories
Active Kinases, Cell Biology, Cell Signaling and Neuroscience, Kinase/Phosphatase Biology, Serine/Threonine Kinase Biology, Serine/Threonine PhosphatasesMore... biological source
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