产品名称
CDK4/CyclinD3, active, GST tagged human, PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
recombinant
expressed in baculovirus infected Sf9 cells
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
13-19 nmol/min·mg
mol wt
CDK4 subunit ~58 kDa
cyclin D3 ~58 kDa
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... CCND3(896), CDK4(1019)
Biochem/physiol Actions
CDK4 is a member of the cyclin-dependent protein kinase family and is involved in the control of cell proliferation during the G1 phase of cell cycle. CDK4 forms a complex with the D-type cyclins and is inhibited by p16 (cyclin-dependent kinase inhibitor-2). CDK4 can mediate phosphorylation of the C-terminal region of Rb protein leading to an active transcriptional repression of E2F complex. CDC37 and HSP90 can preferentially associate with the fraction of CDK4 not bound to D-type cyclins. SMAD3 is a major physiologic substrate of the G1 cyclin-dependent kinases CDK4 and CDK2.
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
J W Harbour et al.
Cell, 98(6), 859-869 (1999-09-28)
We present evidence that phosphorylation of the C-terminal region of Rb by Cdk4/6 initiates successive intramolecular interactions between the C-terminal region and the central pocket. The initial interaction displaces histone deacetylase from the pocket, blocking active transcriptional repression by Rb.
Isao Matsuura et al.
Nature, 430(6996), 226-231 (2004-07-09)
Transforming growth factor-beta (TGF-beta) potently inhibits cell cycle progression at the G1 phase. Smad3 has a key function in mediating the TGF-beta growth-inhibitory response. Here we show that Smad3 is a major physiological substrate of the G1 cyclin-dependent kinases CDK4
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