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Merck
CN

C7620

Sigma-Aldrich

CLK2 (137-end), active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

别名:

MGC61500, hCLK2

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关于此项目

UNSPSC代码:
12352200
NACRES:
NA.32
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重组

expressed in baculovirus infected Sf9 cells

质量水平

产品线

PRECISIO® Kinase

方案

≥70% (SDS-PAGE)

表单

buffered aqueous glycerol solution

比活

45-60 nmol/min·mg

分子量

~68 kDa

UniProt登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... CLK2(1196)

生化/生理作用

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.

外形

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.

法律信息

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

新产品
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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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