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Principaux documents

14-349

Sigma-Aldrich

MAPKAP Kinase 2 Protein, inactive, 50 g

Unactive, For use in Kinase Assays.

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About This Item

Code UNSPSC :
12352202
eCl@ss :
32160405
Nomenclature NACRES :
NA.41

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Poids mol.

Mw 66 kDa

Fabricant/nom de marque

Upstate®

Technique(s)

activity assay: suitable (kinase)

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Informations sur le gène

human ... MAPKAPK2(9261)

Description générale

Product Source: Expressed in E.coli
Recombinant human MAPKAP Kinase 2 (MAPKAP-K2), residues 46-400, A399G, containing an N-terminal GST tag

MAPKAP Kinase 2 has been implicted as a cell cycle checkpoint kinase, joining the ranks of Chk1 and Chk2 as critical regulators of the DNA damage response in mammalian cells in recent studies (Manke, et al, 2005, and Abraham, 2005). This research indicates that MAPKAP Kinase 2, a serine/threonine kinase activated by p38, phosphorylates CDC25 B/C, generating a binding site for 14-3-3 proteins. The checkpoint kinases Chk1 and Chk2 are targets for drug discovery efforts designed to overcome cell cycle arrest due to DNA damage induced by chemotherapeutic agents. Overriding the checkpoint kinases in cancer cells exposed to DNA damaging agents leads to catastrophic failure of cell division and apoptosis.
The new role of MAPKAP Kinase 2 in complementing the function of Chk1 and Chk2 suggests a new target for drug discovery efforts.

Actions biochimiques/physiologiques

Protein Target: MAPKAP-K2
Target Sub-Family: CAMK

Qualité

Routinely evaluated by phosphorylation of MAPKAP-K2 substrate peptide

Forme physique

Glutathione-agarose

Stockage et stabilité

6 months at -20°C

Autres remarques

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

Informations légales

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Skin Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Y Hefner et al.
The Journal of biological chemistry, 275(48), 37542-37551 (2000-09-09)
We have previously reported that in thrombin-stimulated human platelets, cytosolic phospholipase A(2) (cPLA2) is phosphorylated on Ser-505 by p38 protein kinase and on Ser-727 by an unknown kinase. Pharmacological inhibition of p38 leads to inhibition of cPLA2 phosphorylation at both
Bart S Hendriks et al.
BMC systems biology, 4, 23-23 (2010-03-17)
The success of anti-TNF biologics for the treatment of rheumatoid arthritis has highlighted the importance of understanding the intracellular pathways that regulate TNF production in the quest for an orally-available small molecule inhibitor. p38 is known to strongly regulate TNF
D Stokoe et al.
The Biochemical journal, 296 ( Pt 3), 843-849 (1993-12-15)
The substrate specificity of mitogen-activated protein (MAP) kinase-activated protein kinase-2 (MAPKAP kinase-2) was investigated by using synthetic peptides related to the N-terminus of glycogen synthase. The minimum sequence required for efficient phosphorylation was found to be Xaa-Xaa-Hyd-Xaa-Arg-Xaa-Xaa-Ser-Xaa-Xaa, where Hyd is
A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway.
Ben-Levy, R, et al.
The Embo Journal, 13, 3302-3311 (1994)
D Stokoe et al.
The EMBO journal, 11(11), 3985-3994 (1992-11-01)
A novel protein kinase, which was only active when phosphorylated by the mitogen-activated protein kinase (MAP kinase), has been purified 85,000-fold to homogeneity from rabbit skeletal muscle. This MAP kinase activated protein kinase, termed MAPKAP kinase-2, was distinguished from S6

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