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Peptidylprolyl Isomerase Active Protein | PPIL1 active protein

Recombinant Human Peptidylprolyl Isomerase (Cyclophilin)-Like 1

Gene Names
PPIL1; CYPL1; hCyPX; PPIase; CGI-124
Purity
Greater than 95.0% as determined by SDS-PAGE.
Synonyms
Peptidylprolyl Isomerase; Recombinant Human Peptidylprolyl Isomerase (Cyclophilin)-Like 1; PPIL1 Human; Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant; Peptidyl-Prolyl Cis-Trans Isomerase-Like 1; PPIL-1; CYPL1; hCyPX; MGC678; PPIase; CGI-124; PPIL1; PPIL1 active protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater than 95.0% as determined by SDS-PAGE.
Form/Format
PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol
Sterile filtered colorless solution.
Sequence
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH
Sequence Length
166
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.
Preparation and Storage
PPIL1 Human Recombinant although stable at 4 degree C for 1 week, should be stored desiccated below -18 degree C. Please prevent freeze thaw cycles.
Related Product Information for PPIL1 active protein
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.

Introduction: 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.
Product Categories/Family for PPIL1 active protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
18,237 Da
NCBI Official Full Name
peptidyl-prolyl cis-trans isomerase-like 1
NCBI Official Synonym Full Names
peptidylprolyl isomerase (cyclophilin)-like 1
NCBI Official Symbol
PPIL1
NCBI Official Synonym Symbols
CYPL1; hCyPX; PPIase; CGI-124
NCBI Protein Information
peptidyl-prolyl cis-trans isomerase-like 1; cyclophilin-related gene 1; rotamase PPIL1
UniProt Protein Name
Peptidyl-prolyl cis-trans isomerase-like 1
Protein Family
UniProt Gene Name
PPIL1
UniProt Synonym Gene Names
CYPL1; PPIase
UniProt Entry Name
PPIL1_HUMAN

NCBI Description

This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [provided by RefSeq, Jul 2008]

Uniprot Description

PPIL1: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily.

Protein type: Cyclophilin; Isomerase; EC 5.2.1.8; Spliceosome

Chromosomal Location of Human Ortholog: 6p21.1

Molecular Function: protein binding; peptidyl-prolyl cis-trans isomerase activity

Biological Process: nuclear mRNA splicing, via spliceosome; protein peptidyl-prolyl isomerization; protein folding

Research Articles on PPIL1

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Product Notes

The PPIL1 ppil1 (Catalog #AAA143576) is an Active Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGL EHH HHHH. It is sometimes possible for the material contained within the vial of "Peptidylprolyl Isomerase, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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