生物来源
human
质量水平
重组
expressed in E. coli Human MAPKAP Kinase
expressed in E. coli
产品线
Upstate®
比活
(For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.)
分子量
Mw 70.2 kDa
纯化方式
(GSH-agarose & Q-Sepharose FF)
种属反应性
human
制造商/商品名称
Upstate®
技术
activity assay: suitable (kinase)
登记号
(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登记号
UniProt登记号
基因信息
human ... MAPKAPK2(9261)
一般描述
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.
生化/生理作用
Protein Target: MAPKAP-K2
Target Sub-Family: CAMK
包装
Also available in 10 μg size and in bulk
Also available in 250μg size as catalog # 14-337M - Call for pricing and availability.
质量
Routinely evaluated by phosphorylation of MAPKAP Kinase 2 Substrate Peptide
目标描述
MAPKAP-K2
外形
GSH-agarose & Q-Sepharose FF
储存及稳定性
1 year at -20°C
其他说明
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
法律信息
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
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.
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.
警示用语：
Warning
危险声明
危险分类
Skin Sens. 1
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 1
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
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
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
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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