SRP0246
LKB1/MO25/STRAD Active human
recombinant, expressed in baculovirus infected insect cells, ≥70% (SDS-PAGE)
Sinónimos:
STK11, Serine/threonine kinase 11
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About This Item
Código UNSPSC:
12352204
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad
Productos recomendados
origen biológico
human
recombinante
expressed in baculovirus infected insect cells
Ensayo
≥70% (SDS-PAGE)
Formulario
aqueous solution
mol peso
49 kDa (LKB1)
66 kDa (MO25)
74 kDa (STRAD)
envase
pkg of 20 μg
condiciones de almacenamiento
avoid repeated freeze/thaw cycles
concentración
>0.02 mg/mL
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... STK11(6794)
Descripción general
The product is a complex of human Liver kinase B1 (LKB1), also known as serine/threonine kinase 11 (STK11) (GenBank Accession No. NM_000455; amino acids 2-433, with N-terminal His-tag), mouse protein- 25 (MO25) or calcium binding protein 39 (CAB39) (GenBank Accession No. NM_016289; amino acids 2-341, with N-terminal GST-tag) and STE20-related kinase adaptor alpha (STRAD) (GenBank Accession No. NM_001003787, a.a. 2-431, with N-terminal GST-tag).
Aplicación
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Acciones bioquímicas o fisiológicas
Liver kinase B1 (LKB1), also known as serine/threonine kinase 11 (STK11), is a serine/threonine kinase that regulates cell polarity and functions as a tumor suppressor protein. LKB1 regulates the activity of adenosine monophosphate-activated protein kinase (AMPK), promoting the suppression of growth and proliferation under energetically unfavorable conditions. Mouse protein-25 (MO25) or calcium binding protein 39 (CAB39) is a scaffolding protein which modulates the activities of STE20 family protein kinases. The MO25a isoform is part of the LKB1 tumor suppressor complex.[1] STE20-related kinase adaptor α (STRAD) is a pseudokinase. It forms a heterotrimeric complex with LKB1 and MO25. The LKB1/MO25/STRAD complex modulates the metabolism, proliferation and cellular polarity of human intestinal epithelial cells.[2]
Forma física
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.
Nota de preparación
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Structural insights into the activation of MST3 by MO25.
Mehellou Y
Biochemical and Biophysical Research Communications, 431(3), 604-609 (2013)
P A Marignani et al.
Cancer biology & therapy, 6(10), 1627-1631 (2007-10-09)
STRADalpha is a pseudokinase that forms a heterotrimeric complex with the scaffolding protein MO25 and the tumor suppressor serine threonine protein kinase LKB1. Mutations in the LKB1 gene are responsible for the Peutz-Jeghers Syndrome (PJS) characterized by a predisposition to
Naomi X Y Ling et al.
Nature metabolism, 2(1), 41-49 (2020-01-30)
Central to cellular metabolism and cell proliferation are highly conserved signalling pathways controlled by mammalian target of rapamycin (mTOR) and AMP-activated protein kinase (AMPK)1,2, dysregulation of which are implicated in pathogenesis of major human diseases such as cancer and type
Yue Zong et al.
Cell research, 29(6), 460-473 (2019-04-06)
AMPK, a master regulator of metabolic homeostasis, is activated by both AMP-dependent and AMP-independent mechanisms. The conditions under which these different mechanisms operate, and their biological implications are unclear. Here, we show that, depending on the degree of elevation of
Kuo-Hui Su et al.
Molecular cell, 76(4), 546-561 (2019-09-29)
Through transcriptional control of the evolutionarily conserved heat shock, or proteotoxic stress, response, heat shock factor 1 (HSF1) preserves proteomic stability. Here, we show that HSF1, a physiological substrate for AMP-activated protein kinase (AMPK), constitutively suppresses this central metabolic sensor.
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