C1245
CLK1 (129-end), active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
CLK/STY, STY
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10 μG
€494.00
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10 μG
€494.00
About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
170-230 nmol/min·mg
mol wt
~66 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CLK1(1195)
Biochem/physiol Actions
CLK/STY is a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. The phosphorylated serine/arginine-rich (SR) proteins involves in the pre-mRNA processing and releasing through nucleus into nucleoplasm. CLK/STY, which could phosphorylates the specific SR proteins, such as ASF/SF2, may directly regulates the activity and compartmentalization of SR splicing factors.
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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K Colwill et al.
The Journal of biological chemistry, 271(40), 24569-24575 (1996-10-04)
Serine/arginine-rich (SR) proteins are essential for pre-mRNA splicing, and modify the choice of splice site during alternative splicing in a process apparently regulated by protein phosphorylation. Two protein kinases have been cloned that can phosphorylate SR proteins in vitro: SRPK1
Jayendra Prasad et al.
Molecular and cellular biology, 23(12), 4139-4149 (2003-05-30)
SR proteins constitute a family of splicing factors that play key roles in both constitutive and regulated splicing in metazoan organisms. The proteins are extensively phosphorylated, and kinases capable of phosphorylating them have been identified. However, little is known about
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