PPIH Human
Cyclophilin-H Human Recombinant
Cat. No.
BT3833
Source
Escherichia Coli.
Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa.
PPIH is purified by proprietary chromatographic techniques.
PPIH is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Belonging to the peptidyl-prolyl cis-trans isomerase (PPIase) family, PPIH catalyzes the cis-trans isomerization of proline imidic peptide bonds within oligopeptides, thereby accelerating protein folding. This enzyme plays a crucial role in the complex comprising pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, along with U4/U5/U6 tri-snRNP. Exhibiting PPIase activity, PPIH functions as a protein chaperone, facilitating interactions between different proteins within the spliceosome.
Description
Recombinant human PPIH, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 177 amino acids (1-177) and has a molecular weight of 19.2 kDa. The purification of PPIH is achieved using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The solution contains 1 mg of PPIH per ml in 1x PBS buffer at pH 7.4 with 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the solution refrigerated at 4°C. For extended storage, freeze the solution at -20°C. To ensure optimal stability during long-term storage, adding a carrier protein like HSA or BSA (0.1%) is recommended. Avoid repeated freeze-thaw cycles.
Biological Activity
The specific activity, determined as the amount of enzyme required to cleave 1 µmol of suc-AAFP-pNA per minute at 25°C and pH 8.0 in Tris-HCl buffer using chymotrypsin, is greater than 220 nmol/min/mg.
Purity
PPIH purity exceeds 95.0%, as confirmed by both reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
Source
Escherichia Coli.
Amino Acid Sequence
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.
Product Science Overview
Structural and Functional Characteristics
Cyclophilin-H is a specific component of the human spliceosome, a complex responsible for the removal of introns from pre-mRNA. It plays a crucial role in the splicing of pre-mRNA by interacting with other spliceosomal proteins and RNA . The enzyme’s activity is essential for the proper folding and function of proteins, making it a vital player in cellular processes.
Recombinant Cyclophilin-H
Recombinant human Cyclophilin-H is produced using recombinant DNA technology, which involves inserting the gene encoding Cyclophilin-H into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of the protein for research and therapeutic purposes .
Applications in Research and Medicine
Cyclophilin-H has been studied extensively for its role in various cellular processes and its potential therapeutic applications. Some key areas of research and application include:
- Protein Folding: Cyclophilin-H assists in the proper folding of proteins, which is crucial for their function. Misfolded proteins can lead to various diseases, including neurodegenerative disorders.
- Spliceosome Function: As a component of the spliceosome, Cyclophilin-H is essential for the accurate splicing of pre-mRNA, a critical step in gene expression.
- Drug Target: Cyclophilins, including Cyclophilin-H, are targets for immunosuppressive drugs like cyclosporin A, which is used to prevent organ transplant rejection .
- Disease Research: Understanding the function and regulation of Cyclophilin-H can provide insights into diseases related to protein misfolding and splicing defects.
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