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Merck
CN

SRP5084

Sigma-Aldrich

ROS1(1883-端),活性,GST 标记 人

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

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别名:
MCF3, ROS, c-ros-1
UNSPSC代码:
12352200
NACRES:
NA.32

重组

expressed in baculovirus infected Sf9 cells

产品线

PRECISIO® Kinase

检测方案

≥70% (SDS-PAGE)

形式

buffered aqueous glycerol solution

比活

544-736 nmol/min·mg

分子量

~82 kDa

NCBI登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... ROS1(6098)

一般描述

ROS1 is a proto-oncogene and member of the sevenless subfamily of tyrosine kinase insulin receptor genes. ROS1 is highly-expressed in a variety of tumor cell lines and functions as a growth or differentiation factor receptor. The FIG gene can fuse with the ROS1 gene in glioblastoma cell lines. The resulting ROS1/FIG fusion protein is a constitutively activated tyrosine kinase. Direct interaction of ROS1 and the phosphatase SHP-1 can lead to efficient downregulation of ROS1-mediated signaling. Binding sites in the ROS1 cytoplasmic domain display high affinity binding to the SHP-1 N-terminal SH2 domain.

外形

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

制备说明

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

法律信息

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

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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Christoph Biskup et al.
Journal of cell science, 117(Pt 21), 5165-5178 (2004-10-01)
Signaling of receptor tyrosine kinases (RTKs) is regulated by protein-tyrosine phosphatases (PTPs). We previously discovered the efficient downregulation of Ros RTK signaling by the SH2 domain PTP SHP-1, which involves a direct interaction of both molecules. Here, we studied the
Alain Charest et al.
Genes, chromosomes & cancer, 37(1), 58-71 (2003-03-28)
The transmembrane proto-oncogene receptor tyrosine kinase (RTK) ROS is an orphan receptor that is aberrantly expressed in neoplasms of the central nervous system. Here, we report the fusion of its carboxy-terminal kinase domain to the amino-terminal portion of a protein

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