S6698
SRPK1, active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
SFSK1
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About This Item
Recommended Products
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
173-234 nmol/min·mg
mol wt
~130 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... SRPK1(6732)
Biochem/physiol Actions
SRPK1 is a Ser/Thr protein kinase that has sequence and function similar to SRPK2. In human cancer cells, it was observed that inactivation of SRPK1 induces cellular resistance to anticancer drugs such as cisplatin and bleomycin. SRPK1 phosphorylates serine/arginine-rich (SR) proteins, such as splicing factors ASF/SF2, SC35, and SRp55, in their arginine/serine-rich (RS) domains in vitro. Hence it is believed that SRPK1 plays a key role in regulation of both constitutive and alternative splicing by regulating intracellular localization of 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
Certificates of Analysis (COA)
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Nature, 369(6482), 678-682 (1994-06-23)
Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP splicing factors containing a serine/arginine-rich domain (SR proteins) concentrate in 'speckles' in the nucleus of interphase cells. It is believed that nuclear speckles act as storage sites for splicing factors while splicing occurs
Cancer research, 67(5), 2072-2080 (2007-03-03)
Aberrant patterns of pre-mRNA processing are typical of human malignancies, yet the mechanisms responsible for these changes remain undefined. We have recently shown overexpression of a core splice regulatory protein, serine-arginine protein kinase 1 (SRPK1), in dysplastic and neoplastic pancreatic
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