产品名称
MAPKAP Kinase 2 Protein, active, 10 µg, Active, for use in Kinase Assays.
biological source
human
recombinant
expressed in E. coli Human MAPKAP Kinase
expressed in E. coli
product line
Upstate®
specific activity
(For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.)
mol wt
Mw 70.2 kDa
purified by
(GSH-agarose & Q-Sepharose FF)
species reactivity
human
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
accession no.
(FUNCTION: SwissProt: P49137 # Its physiological substrate seems to be the small heat shock protein (HSP27/HSP25). In vitro can phosphorylate glycogen synthase at ′Ser-7′ and tyrosine hydroxylase (on ′Ser-19′ and ′Ser-40′). This kinase phosphorylates Ser in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue (By similarity). Mediates both ERK and p38 MAPK/MAPK14 dependent neutrophil responses. Participates in TNF alpha-stimulated exocytosis of secretory vesicles in neutrophils. Plays a role in phagocytosis-induced respiratory burst activity. )
NM_004759.3
NCBI accession no.
UniProt accession no.
Quality Level
Gene Information
human ... MAPKAPK2(9261)
Analysis Note
Routinely evaluated by phosphorylation of MAPKAP Kinase 2 Substrate Peptide
Biochem/physiol Actions
Protein Target: MAPKAP-K2
Target Sub-Family: CAMK
Disclaimer
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.
General description
MAPKAP-K2
Product Source: Human MAPKAP Kinase 2 expressed in E. coli.
Recombinant human MAPKAP Kinase 2, 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.
This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.
Other Notes
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Packaging
Also available in 10 μg size and in bulk
Also available in 250μg size as catalog # 14-337M - Call for pricing and availability.
Physical form
GSH-agarose & Q-Sepharose FF
Preparation Note
1 year at -20°C
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
signalword
Warning
hcodes
Hazard Classifications
Skin Sens. 1
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
J Xu et al.
The Biochemical journal, 355(Pt 2), 437-447 (2001-04-04)
When fibroblasts are cultured in contracting collagen matrices, matrix metalloproteinase-1 (MMP-1, collagenase-1) is induced. In the present study we demonstrate that p38alpha mitogen-activated protein kinase (p38alpha MAPK) plays a bi-directional role in the MMP-1 response to contracting floating collagen lattices
Madhavi J Rane et al.
The Journal of biological chemistry, 278(30), 27828-27835 (2003-05-13)
Activation of the serine-threonine kinase Akt by cytokines, chemokines, and bacterial products delays constitutive neutrophil apoptosis, resulting in a prolonged inflammatory response. We showed previously that Akt exists in a signaling complex with p38 MAPK, MAPK-activated protein kinase-2 (MAPKAPK-2), and
Y L Woods et al.
The Biochemical journal, 355(Pt 3), 597-607 (2001-04-20)
Forkhead in rhabdomyosarcoma (FKHR) is a transcription factor that has been implicated in the control of gene expression by insulin, as well as the regulation of apoptosis by survival factors. These signals trigger the protein kinase B (PKB)-catalysed phosphorylation of
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)
M Suomalainen et al.
The EMBO journal, 20(6), 1310-1319 (2001-03-17)
Nuclear targeting of adenovirus is mediated by the microtubule-dependent, minus-end-directed motor complex dynein/dynactin, in competition with plus- end-directed motility. We demonstrate that adenovirus transiently activates two distinct signaling pathways to enhance nuclear targeting. The first pathway activates integrins and cAMP-dependent
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