14-349
MAPKAP Kinase 2 Protein, inactive, 50 g
Unactive, For use in Kinase Assays.
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About This Item
UNSPSC-Code:
12352202
eCl@ss:
32160405
NACRES:
NA.41
Biologische Quelle
human
Qualitätsniveau
Rekombinant
expressed in E. coli
Mol-Gew.
Mw 66 kDa
Hersteller/Markenname
Upstate®
Methode(n)
activity assay: suitable (kinase)
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Angaben zum Gen
human ... MAPKAPK2(9261)
Allgemeine Beschreibung
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.
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.
Biochem./physiol. Wirkung
Protein Target: MAPKAP-K2
Target Sub-Family: CAMK
Qualität
Routinely evaluated by phosphorylation of MAPKAP-K2 substrate peptide
Physikalische Form
Glutathione-agarose
Lagerung und Haltbarkeit
6 months at -20°C
Sonstige Hinweise
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Rechtliche Hinweise
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Haftungsausschluss
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.
Signalwort
Warning
H-Sätze
Gefahreneinstufungen
Skin Sens. 1
Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 2
Analysenzertifikate (COA)
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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
Qamraa H Al-Qahtani et al.
Molecular oncology, 15(8), 2120-2139 (2021-01-08)
Dysfunctions in post-transcriptional control are observed in cancer and chronic inflammatory diseases. Here, we employed a kinome inhibitor library (n = 378) in a reporter system selective for 3'-untranslated region-AU-rich elements (ARE). Fifteen inhibitors reduced the ARE-reporter activity; among the targets 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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