|Calculated MW||21.6 kDa|
|Other Names||Peptidyl-prolyl cis-trans isomerase G, PPIase G, Rotamase G, PPIG, peptidylprolyl isomerase G, Peptidyl-prolyl isomerase G, Rotamase G, Clk-associating RS-cyclophilin, CARS-cyclophilin, CARS-Cyp, SR-cyclophilin, SR-cyp, SRcyp, CASP10, CYP, MGC133241.|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCG|
|Storage||-80°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, and 10% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Peptidyl-prolyl cis-trans isomerase G (PPIG), also known as Cyclophilin G, is a member of peptidylprolyl cis-trans isomerase family (PPIases). This protein catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and is implicated in the folding, transport, and assembly of proteins. It is localized to the nuclear speckles, a nuclear compartment rich in splicing factors, and interacts with the splicing factors SC35 and pinin. Cyclophilin G also may play an important role in the regulation of pre-mRNA splicing.
Nestel F.P.,et al.Gene 180:151-155(1996).
Bourquin J.-P.,et al.Nucleic Acids Res. 25:2055-2061(1997).
Hillier L.W.,et al.Nature 434:724-731(2005).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Lin C.L.,et al.Biochem. Biophys. Res. Commun. 321:638-647(2004).
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