Nucleotide Analogs - Jena Bioscience

Recombinant Proteins
172
Splicing Factor Proteins
Transcription and pre-mRNA splicing are
tightly coupled gene expression events in
eukaryotic cells. An interaction between the
carboxy-terminal domain of the largest subunit
of RNA Polymerase (Pol) II and components
of the splicing machinery is postulated to
mediate this coupling. Splicing takes place
in the spliceosome, a large RNA–protein
complex composed of various small nuclear
ribonucleoprotein particles (snRNPs), and many
other proteins. These so called splicing factors
function directly to promote the transcriptional
elongation.
ASF/SF2 (SFRS1 or SRp30a)
(Pre-mRNA Splicing Factor)
human, Recombinant, E. coli
Cat. No. Amount Price (€)
PR-774 10 µg 350,--
Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM
KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol.
ASF or called SF2, a member of SR protein family, is
an essential pre-mRNA splicing factor required for both
single and alternative splicing. Phosphorylation on
serine residues located within the SR domain directly
regulates ASF/SF2 activity and compartmentalization
of other SR splicing factors. In addition to interacting
with RNA and other splicing factors, such as U1-70K,
U2AF and other SR proteins, ASF/SF2 also directly or
indirectly interacts with HIV regulatory protein Rev, the
C-terminal domain (CTD) of the largest subunit of RNA
Polymerase II, and numerous transcription factors,
thereby suggesting a potential role of ASF/SF2 in
coordinating of transcription and pre-mRNA splicing.
The human ASF/SF2 wild type protein (residue 1-248)
was expressed in E. coli and purifi ed by an affi nity
column.
Recombinant ASF/SF2 protein can be used 1) for in
vitro function studies including pre-mRNA splicing,
cross linking and other RNA binding assays; 2) for
protein-protein interaction assay; and 3) for cell growth
and proliferation assays.
Purifi ed protein is greater than 95% homogeneous
and contains no detectable proteases, DNase and
RNase activity.
Unit defi nition:
1 unit equals 1 ng of purifi ed protein. 1 unit is suffi cient
for a gel mobility shift assay in a 20 µl reaction and
100 units are suffi cient for a protein-protein interaction
assay.
Purity: > 95% by SDS-PAGE.
Store: -80 °C
Selected references:
Ge et al. (1990) A protein factor, ASF, controls cell-specifi c
alternative splicing of SV40 early pre-mRNA in vitro. Cell 62:
25.
Ge et al. (1991) Primary structure of the human splicing factor
ASF reveals similarities with Drosophila regulators. Cell 66:
373.
Krainer et al. (1990) The essential pre-mRNA splicing factor
SF2 infl uences 5’ splice site selection by activating proximal
sites. Cell 62:35.
Krainer et al. (1991) Functional expression of cloned human
splicing factor SF2: homology to RNA-binding proteins, U1 70K,
and Drosophila splicing regulators. Cell 66:383.
Zahler et al. (1992) SR proteins: a conserved family of premRNA
splicing factors. Genes & Dev. 6:837.
Gui et al. (1994) Purifi cation and characterization of a kinase
specifi c for the serine- and arginine-rich pre-mRNA splicing
factors. Proc. Natl. Acad. Sci. USA 91:10824.
Colwill et al. (1996) The Clk/Sty protein kinase phosphorylates
SR splicing factors and regulates their intranuclear distribution.
EMBO J. 15:265.
Tange et al. (1996) In vitro interaction between human
immunodefi ciency virus type 1 Rev protein and splicing factor
ASF/SF2-associated protein, p32. J. Biol. Chem. 271:10066.
ASF/SF2 (SFRS1 or SRp30a)
(Pre-mRNA Splicing Factor)
human, Recombinant, Sf9
insect cells
Cat. No. Amount Price (€)
PR-775 5 µg 450,--
Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM
KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol.
ASF or called SF2, a member of SR protein family, is
an essential pre-mRNA splicing factor required for both
single and alternative splicing. Phosphorylation on
serine residues located within the SR domain directly
regulates ASF/SF2 activity and compartmentalization
of other SR splicing factors. In addition to interacting
with RNA and other splicing factors, such as U1-70K,
U2AF and other SR proteins, ASF/SF2 also directly or
indirectly interacts with HIV regulatory protein Rev, the
C-terminal domain (CTD) of the largest subunit of RNA
Polymerase II, and numerous transcription factors,
thereby suggesting a potential role of ASF/SF2 in
coordinating of transcription and pre-mRNA splicing.
The human ASF/SF2 wild type protein (residue 1-248)
was expressed in baculovirus system and purifi ed
by an affi nity column in combination with FPLC
chromatography.
Recombinant ASF/SF2 protein can be used 1) for in
vitro function studies including pre-mRNA splicing,
cross linking and other RNA binding assays; 2) for
protein-protein interaction assay; and 3) for cell growth
and proliferation assays.
Purifi ed protein is greater than 95% homogeneous
and contains no detectable proteases, DNase, and
RNase activity.
Unit defi nition:
1 unit equals 1 ng of purifi ed protein. 1 unit is suffi cient
for a gel mobility shift assay in a 20 µl reaction and
100 units are suffi cient for a protein-protein interaction
assay.
Purity: > 95% by SDS-PAGE.
Store: -80 °C
Selected references:
Ge et al. (1991) Primary structure of the human splicing factor
ASF reveals similarities with Drosophila regulators. Cell 66:
373.
Krainer et al. (1990) The essential pre-mRNA splicing factor
SF2 infl uences 5’ splice site selection by activating proximal
sites. Cell 62:35.
Zahler et al. (1992) SR proteins: a conserved family of premRNA
splicing factors. Genes & Dev. 6:837.
Gui et al. (1994) Purifi cation and characterization of a kinase
specifi c for the serine- and arginine-rich pre-mRNA splicing
factors. Proc. Natl. Acad. Sci. USA 91:10824.
Colwill et al. (1996) The Clk/Sty protein kinase phosphorylates
SR splicing factors and regulates their intranuclear distribution.
EMBO J. 15:265.
Tange et al. (1996) In vitro interaction between human
immunodefi ciency virus type 1 Rev protein and splicing factor
ASF/SF2-associated protein, p32. J. Biol. Chem. 271:10066.
SC35 (SFRS2 or SRp30b)
(Pre-mRNA Splicing Factor)
human, Recombinant, Sf9
insect cells
Cat. No. Amount Price (€)
PR-776 5 µg 400,--
Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM
KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol.
SC35, a member of SR protein family, is an essential
pre-mRNA splicing factor. Phosphorylation on serine
residues located within the SR domain directly
regulates SC35 activity and compartmentalization of
other SR splicing factors. In addition to interacting with
RNA and other splicing factors, SC35 has been shown
http://www.jenabioscience.com
to interact either directly or indirectly interacts with the
C-terminal domain (CTD) of the largest subunit of RNA
Polymerase II, thereby suggesting a potential role of
SC35 in coordinating of transcription and pre-mRNA
splicing.
The human SC35 wild type protein was expressed in
baculovirus system and purifi ed by an affi nity column
in combination with FPLC chromatography.
Recombinant SC35 protein can be used 1) for in vitro
function studies including pre-mRNA splicing, cross
linking and other RNA binding assays; 2) for proteinprotein
interaction assay; and 3) for cell growth and
proliferation assays.
Purifi ed protein is greater than 95% homogeneous
and contains no detectable proteases, DNase, and
RNase activity.
Unit defi nition:
1 unit equals 1 ng of purifi ed protein. 1 unit is the
amount suffi cient for a gel mobility shift assay in a
20 µl reaction 50 and 100 units are suffi cient for a
protein-protein interaction assay.
Purity: > 95% by SDS-PAGE.
Store: -80 °C
Selected references:
Fu et al. (1992) Isolation of a complementary DNA that encodes
the mammalian splicing factor SC35. Science 256:535.
Zahler et al. (1992) SR proteins: a conserved family of premRNA
splicing factors. Genes & Dev. 6:837.
Gui et al. (1994) Purifi cation and characterization of a kinase
specifi c for the serine- and arginine-rich pre-mRNA splicing
factors. Proc. Natl. Acad. Sci. USA 91:10824.
Colwill et al. (1996) The Clk/Sty protein kinase phosphorylates
SR splicing factors and regulates their intranuclear distribution.
EMBO J. 15:265.
Misteli et al. (1997) The dynamics of a pre-mRNA splicing factor
in living cells. Nature 387:523.
Nuclear Receptor
Proteins
Nuclear receptors regulate gene expression in
response to binding small lipophilic molecules
and are thereby involved in the control of a
diversity of cellular processes. These proteins
are ligand-activated transcription factors that
are localized in the cytosol and/or the nucleus
(also called soluble receptors). The hormone
ligands pass the cell membrane by simple
diffusion and bind to the cognate receptors in
the cytoplasm or in the nucleus. By binding
to cognate DNA sequences termed hormone
responsive elements (HREs) the ligand-bound
receptor activates target genes and thus
transmits hormonal signals into a change of
gene expression.
In contrast to heterodimeric nuclear receptors,
which are located exclusively in the nucleus,
homodimeric receptors are found both in the
cytoplasm and nucleus, and their activity is
regulated by controlling their transport from the
cytoplasm to the nucleus.
ER (Estrogen Receptor)
human, Recombinant, Sf9
insect cells
Cat. No. Amount Price (€)
PR-756 4 µg 450,--
Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM
KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol.
Several members of nuclear receptor family are
directly associated with human malignancies including
breast cancer, prostate cancer and leukemia.
The pathogenesis of each of these diseases is
underpinned by the activities of a member of the
superfamily; Estrogen Receptor-alpha (ER-α) in