|Calculated MW||59.4 kDa|
|Other Names||Peptidyl-prolyl cis-trans isomerase-like 4, HDCME13P, Rotamase PPIL4, Cyclophilin-like protein PPIL4.|
|Sequence||MGSSHHHHHH SSGLVPRGSH MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR|
|Storage||-80°C; 0.5 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol, 2 mM DTT and 0.1 M NaCl.|
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Provided below are standard protocols that you may find useful for product applications.
PPIL4 is an evolutionarily conserved member of the cyclophilin-type PPIase family of proteins. Ubiquitously expressed with predominant expression in kidney, PPIL4 localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences suggests that PPIL4 may be involved in transcriptional regulation.
Zeng L.,et al.Cytogenet. Cell Genet. 95:43-47(2001).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Bechtel S.,et al.BMC Genomics 8:399-399(2007).
Mungall A.J.,et al.Nature 425:805-811(2003).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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