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Recombinant Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1/PPIase/PPIL1

Recombinant Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1/PPIase/PPIL1 Recombinant Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1/PPIase/PPIL1

Instruction Manual!

Product name: Recombinant Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1/PPIase/PPIL1
Source:E.coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, pH 8.0.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E.coli
Description Recombinant Human PPIase is produced by our E.coli expression system and the target gene encoding Met1-Gly166 is expressed with a 6His tag at the N-terminus.
Names Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIase, Rotamase PPIL1, PPIL1, CYPL1
Accession # Q9Y3C6
Formulation Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, pH 8.0.
Shipping The product is shipped on dry ice/ice packs.
Storage Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSHMAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARR GYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGS QFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG
Background Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family. PPIases can accelerate the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIase is a ubiquitous protein and has highly expression in heart ,skeletal and muscle. PPIase contains a PPIase cyclophilin-type domain and four Cyclosporin A binding regions. PPIase might play an important role in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is suggested that PPIase can act as as a novel molecular target for colon-cancer therapy.

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