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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Specific activity:
45-60 nmol/min·mg
Assay:
≥70% (SDS-PAGE)
Recombinant:
expressed in baculovirus infected Sf9 cells
Quality Level
recombinant
expressed in baculovirus infected Sf9 cells
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
45-60 nmol/min·mg
mol wt
~68 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CLK2(1196)
Biochem/physiol Actions
CDC-like kinase 2 (CLK2), a family of autophosphorylating kinases termed CLK (CDC2/CDC28-like kinases) was shown to phosphorylate SR proteins and to influence alternative splicing in overexpression systems. Recent findings demonstrated that the CLK kinases activate PTP-1B family members, and this phosphatase may be an important cellular target for CLK action. Mutations in the clk-2 proteins affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length.
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM 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
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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Ning Jiang et al.
The Journal of biological chemistry, 278(24), 21678-21684 (2003-04-03)
Mutations in the clk-2 gene of the nematode Caenorhabditis elegans affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length. clk-2 encodes
O Nayler et al.
The Journal of biological chemistry, 273(51), 34341-34348 (1998-12-16)
Pre-mRNA splicing is catalyzed by a multitude of proteins including serine/arginine-rich (SR) proteins, which are thought to play a crucial role in the formation of spliceosomes and in the regulation of alternative splicing. SR proteins are highly phosphorylated, and their
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