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Safety Information

SRP0246

Sigma-Aldrich

LKB1/MO25/STRAD Active human

recombinant, expressed in baculovirus infected insect cells, ≥70% (SDS-PAGE)

Synonym(s):

STK11, Serine/threonine kinase 11

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20 μG
¥53,690

¥53,690

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Estimated to ship onApril 05, 2025

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20 μG
¥53,690

About This Item

UNSPSC Code:
12352204
NACRES:
NA.32

¥53,690

List Price¥76,700Save 30%

Estimated to ship onApril 05, 2025

New, lower price on this item!
Request a Bulk Order

biological source

human

recombinant

expressed in baculovirus infected insect cells

Assay

≥70% (SDS-PAGE)

form

aqueous solution

mol wt

49 kDa (LKB1)
 66 kDa (MO25)
 74 kDa (STRAD)

packaging

pkg of 20 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

>0.02 mg/mL

NCBI accession no.

NM_000455 (STK11)
NM_001003787 (STRAD)
NM_016289 (MO25)

UniProt accession no.

Q15831

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... STK11(6794)

General description

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).

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Biochem/physiol Actions

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]

Physical form

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.

Preparation Note

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

Cartagena Act

Cartagena Act Listed

JAN Code

SRP0246-20UG:

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Certificates of Analysis (COA)

Lot/Batch Number
4006940724
40069100524
4006900524

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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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