View larger

Peptidylprolyl Isomerase ( Cyclophilin )-Like 1 Human Recombinant ( PPIL1 Human )

DescriptionPPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is

$193.00

Data sheet

Formulation PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol
Purity Greater than 95.0% as determined by SDS-PAGE.
Description PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.
Protein Background PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.
Expression host Escherichia Coli.
Synonyms Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.
Reagent Appearance Sterile filtered colorless solution.
Stability PPIL1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
Amino acid sequence MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH.
Biological Activity Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

© 2024 Novateinbio.com